Abc transporters - Revision history

Nnjm2 at 18:03, 2 December 2015

2015-12-02T18:03:49Z

← Older revision		Revision as of 18:03, 2 December 2015
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	ABC transporters 'are the largest family of [[Membrane\|membrane]] transporters'. ABC transporters are integral proteins, using energy from the [[Hydrolysis\|hydrolysis]] of [[ATP\|ATP]] to pump molecules across the memebrane. These transporters are used to transport small [[Molecules\|molecules]] across the cell membrane. Each ABC traporter contains two [[ATP-binding domain\|ATP-binding domains]] called '''cassettes'''. As ATP binds to the casettes they under go dimerization. Each cassette protrudes into [[Cytosol\|cytosol]]. There are two halves of each transporter, of which they can either be made of a single [[Peptide\|peptide]] or by one or more polypeptides, which form a similiar structure. When ATP isn't present the binding site is expressed on either the [[Intracellular\|intracellular]] or [[Extracellular\|extracellular]] space. As the ATP binds it causes a conformational change in the ABC transporter, which exposes the substrate binding site on the opposite face. As a molecule of [[ATP\|ATP]] is hydrolysed, this is followed by the dissociation of [[ADP\|ADP]]. The ATP hydrolysis returns the transporter to its original form <ref>P. M. Jones A. M. George . (2004). The ABC transporter structure and mechanism: perspectives on recent research. Cellular and Molecular Life Sciences CMLS . Volume 61, p682-699.</ref><ref>B Alberts, A Johnson, J Lewis, Martin Raff, K Raff, K Roberts, P Walter, J Wilson, T Hunt (2008). Molecular Biology of The Cell 5th Edition. New York: Garland Science. p660-p665.</ref>.		ABC transporters 'are the largest family of [[Membrane\|membrane]] transporters'. ABC transporters are integral proteins, using energy from the [[Hydrolysis\|hydrolysis]] of [[ATP\|ATP]] to pump molecules across the memebrane. These transporters are used to transport small [[Molecules\|molecules]] across the cell membrane. Each ABC traporter contains two [[ATP-binding domain\|ATP-binding domains]] called '''cassettes'''. As ATP binds to the casettes they under go dimerization. Each cassette protrudes into [[Cytosol\|cytosol]]. There are two halves of each transporter, of which they can either be made of a single [[Peptide\|peptide]] or by one or more polypeptides, which form a similiar structure. When ATP isn't present the binding site is expressed on either the [[Intracellular\|intracellular]] or [[Extracellular\|extracellular]] space. As the ATP binds it causes a conformational change in the ABC transporter, which exposes the substrate binding site on the opposite face. As a molecule of [[ATP\|ATP]] is hydrolysed, this is followed by the dissociation of [[ADP\|ADP]]. The ATP hydrolysis returns the transporter to its original form <ref>P. M. Jones A. M. George . (2004). The ABC transporter structure and mechanism: perspectives on recent research. Cellular and Molecular Life Sciences CMLS . Volume 61, p682-699.</ref><ref>B Alberts, A Johnson, J Lewis, Martin Raff, K Raff, K Roberts, P Walter, J Wilson, T Hunt (2008). Molecular Biology of The Cell 5th Edition. New York: Garland Science. p660-p665.</ref>.

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150652320 at 17:27, 2 December 2015

2015-12-02T17:27:23Z

← Older revision		Revision as of 17:27, 2 December 2015
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	ABC transporters 'are the largest family of [[Membrane\|membrane]] transporters'. ABC transporters are integral proteins, using energy from the [[Hydrolysis\|hydrolysis]] of [[ATP\|ATP]] to pump molecules across the memebrane. These transporters are used to transport small [[Molecules\|molecules]] across the cell membrane. Each ABC traporter contains two [[ATP-binding domain\|ATP-binding domains]] called cassettes. As ATP binds to the casettes they under go dimerization. Each cassette protrudes into [[Cytosol\|cytosol]]. There are two halves of each transporter, of which they can either be made of a single [[Peptide\|peptide]] or by one or more polypeptides, which form a similiar structure. When ATP isn't present the binding site is expressed on either the [[Intracellular\|intracellular]] or [[Extracellular\|extracellular]] space. As the ATP binds it causes a conformational change in the ABC transporter, which exposes the substrate binding site on the opposite face. As a molecule of [[ATP\|ATP]] is hydrolysed, this is followed by the dissociation of [[ADP\|ADP]]. The ATP hydrolysis returns the transporter to its original form <ref>P. M. Jones A. M. George . (2004). The ABC transporter structure and mechanism: perspectives on recent research. Cellular and Molecular Life Sciences CMLS . Volume 61, p682-699.</ref><ref>B Alberts, A Johnson, J Lewis, Martin Raff, K Raff, K Roberts, P Walter, J Wilson, T Hunt (2008). Molecular Biology of The Cell 5th Edition. New York: Garland Science. p660-p665.</ref>.		ABC transporters 'are the largest family of [[Membrane\|membrane]] transporters'. ABC transporters are integral proteins, using energy from the [[Hydrolysis\|hydrolysis]] of [[ATP\|ATP]] to pump molecules across the memebrane. These transporters are used to transport small [[Molecules\|molecules]] across the cell membrane. Each ABC traporter contains two [[ATP-binding domain\|ATP-binding domains]] called '''cassettes'''. As ATP binds to the casettes they under go dimerization. Each cassette protrudes into [[Cytosol\|cytosol]]. There are two halves of each transporter, of which they can either be made of a single [[Peptide\|peptide]] or by one or more polypeptides, which form a similiar structure. When ATP isn't present the binding site is expressed on either the [[Intracellular\|intracellular]] or [[Extracellular\|extracellular]] space. As the ATP binds it causes a conformational change in the ABC transporter, which exposes the substrate binding site on the opposite face. As a molecule of [[ATP\|ATP]] is hydrolysed, this is followed by the dissociation of [[ADP\|ADP]]. The ATP hydrolysis returns the transporter to its original form <ref>P. M. Jones A. M. George . (2004). The ABC transporter structure and mechanism: perspectives on recent research. Cellular and Molecular Life Sciences CMLS . Volume 61, p682-699.</ref><ref>B Alberts, A Johnson, J Lewis, Martin Raff, K Raff, K Roberts, P Walter, J Wilson, T Hunt (2008). Molecular Biology of The Cell 5th Edition. New York: Garland Science. p660-p665.</ref>.

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150072355 at 23:03, 1 December 2015

2015-12-01T23:03:13Z

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	ABC transporters 'are the largest family of membrane transporters'. ABC transporters are ~~intergral~~ proteins, using energy from the hydrolysis of [[ATP\|ATP]] to pump molecules across the memebrane. These transporters are used to transport small [[~~molecules~~\|molecules]] across the cell membrane. Each ABC traporter contains two [[ATP-binding domain\|ATP-binding domains]] called cassettes. As ATP binds to the casettes they under go dimerization. Each cassette protrudes into [[~~cytosol~~\|cytosol]]. There are two halves of each transporter, of which they can either be made of a single [[~~peptide~~\|peptide]] or my one or more polypeptides, which form a similiar structure. When ATP isn't present the binding site is expressed on either the intracellular or extracellular space. As the ATP binds it causes a conformational change in the ABC transporter, which exposes the ~~substate~~ binding site on the opposite face. As a molecule of [[ATP\|ATP]] is hydrolysed, this is followed by the dissociation of [[ADP\|ADP]]. The ATP hydrolysis returns the transporter to its original form <ref>P. M. Jones A. M. George . (2004). The ABC transporter structure and mechanism: perspectives on recent research. Cellular and Molecular Life Sciences CMLS . Volume 61, p682-699.</ref><ref>B Alberts, A Johnson, J Lewis, Martin Raff, K Raff, K Roberts, P Walter, J Wilson, T Hunt (2008). Molecular Biology of The Cell 5th Edition. New York: Garland Science. p660-p665.</ref>.		ABC transporters 'are the largest family of [[Membrane\|membrane]] transporters'. ABC transporters are integral proteins, using energy from the [[Hydrolysis\|hydrolysis]] of [[ATP\|ATP]] to pump molecules across the memebrane. These transporters are used to transport small [[Molecules\|molecules]] across the cell membrane. Each ABC traporter contains two [[ATP-binding domain\|ATP-binding domains]] called cassettes. As ATP binds to the casettes they under go dimerization. Each cassette protrudes into [[Cytosol\|cytosol]]. There are two halves of each transporter, of which they can either be made of a single [[Peptide\|peptide]] or by one or more polypeptides, which form a similiar structure. When ATP isn't present the binding site is expressed on either the [[Intracellular\|intracellular]] or [[Extracellular\|extracellular]] space. As the ATP binds it causes a conformational change in the ABC transporter, which exposes the substrate binding site on the opposite face. As a molecule of [[ATP\|ATP]] is hydrolysed, this is followed by the dissociation of [[ADP\|ADP]]. The ATP hydrolysis returns the transporter to its original form <ref>P. M. Jones A. M. George . (2004). The ABC transporter structure and mechanism: perspectives on recent research. Cellular and Molecular Life Sciences CMLS . Volume 61, p682-699.</ref><ref>B Alberts, A Johnson, J Lewis, Martin Raff, K Raff, K Roberts, P Walter, J Wilson, T Hunt (2008). Molecular Biology of The Cell 5th Edition. New York: Garland Science. p660-p665.</ref>.

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Nnjm2 at 07:15, 29 November 2013

2013-11-29T07:15:01Z

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	~~ ~~ABC transporters 'are the largest family of membrane transporters' ~~(PM jones AM George 2004)~~ . ABC transporters are intergral proteins, using energy from the hydrolysis of ATP to pump molecules across the memebrane . These transporters are used to transport small molecules across the cell membrane. Each ABC traporter contains two ATP-binding domains called cassettes. As ATP binds to the casettes they under go dimerization. Each cassette protrudes into cytosol. There are two halves of each transporter, of which they can either be made of a single peptide or my one or more polypeptides, which form a similiar structure. When ATP isn't present the binding site is expressed on either the intracellular or extracellular space. As the ATP binds it causes a conformational change in the ABC transporter, which exposes the substate binding site on the opposite face. As a molecule of ATP is hydrolysed, this is followed by the dissociation of ADP. The ATP hydrolysis returns the transporter to its original form (B Alberts 2008).		ABC transporters 'are the largest family of membrane transporters'. ABC transporters are intergral proteins, using energy from the hydrolysis of [[ATP\|ATP]] to pump molecules across the memebrane. These transporters are used to transport small [[molecules\|molecules]] across the cell membrane. Each ABC traporter contains two [[ATP-binding domain\|ATP-binding domains]] called cassettes. As ATP binds to the casettes they under go dimerization. Each cassette protrudes into [[cytosol\|cytosol]]. There are two halves of each transporter, of which they can either be made of a single [[peptide\|peptide]] or my one or more polypeptides, which form a similiar structure. When ATP isn't present the binding site is expressed on either the intracellular or extracellular space. As the ATP binds it causes a conformational change in the ABC transporter, which exposes the substate binding site on the opposite face. As a molecule of [[ATP\|ATP]] is hydrolysed, this is followed by the dissociation of [[ADP\|ADP]]. The ATP hydrolysis returns the transporter to its original form <ref>P. M. Jones A. M. George . (2004). The ABC transporter structure and mechanism: perspectives on recent research. Cellular and Molecular Life Sciences CMLS . Volume 61, p682-699.</ref><ref>B Alberts, A Johnson, J Lewis, Martin Raff, K Raff, K Roberts, P Walter, J Wilson, T Hunt (2008). Molecular Biology of The Cell 5th Edition. New York: Garland Science. p660-p665.</ref>.

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	~~P. M. Jones A. M. George . (2004). The ABC transporter structure and mechanism: perspectives on recent research. Cellular and Molecular Life Sciences CMLS . Volume 61, p682-699.<br>~~

	~~B Alberts, A Johnson, J Lewis, Martin Raff, K Raff, K Roberts, P Walter, J Wilson, T Hunt (2008). Molecular Biology of The Cell 5th Edition. New York: Garland Science. p660-p665.~~

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2013-11-28T23:09:25Z

Created page with " ABC transporters 'are the largest family of membrane transporters' (PM jones AM George 2004) . ABC transporters are intergral proteins, using energy from the hydrolysis of ..."

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ABC transporters 'are the largest family of membrane transporters' (PM jones AM George 2004) . ABC transporters are intergral proteins, using energy from the hydrolysis of ATP to pump molecules across the memebrane . These transporters are used to transport small molecules across the cell membrane. Each ABC traporter contains two ATP-binding domains called cassettes. As ATP binds to the casettes they under go dimerization. Each cassette protrudes into cytosol. There are two halves of each transporter, of which they can either be made of a single peptide or my one or more polypeptides, which form a similiar structure. When ATP isn't present the binding site is expressed on either the intracellular or extracellular space. As the ATP binds it causes a conformational change in the ABC transporter, which exposes the substate binding site on the opposite face. As a molecule of ATP is hydrolysed, this is followed by the dissociation of ADP. The ATP hydrolysis returns the transporter to its original form (B Alberts 2008).

 

 

 

 

References:

 

P. M. Jones A. M. George . (2004). The ABC transporter structure and mechanism: perspectives on recent research. Cellular and Molecular Life Sciences CMLS . Volume 61, p682-699. 

B Alberts, A Johnson, J Lewis, Martin Raff, K Raff, K Roberts, P Walter, J Wilson, T Hunt (2008). Molecular Biology of The Cell 5th Edition. New York: Garland Science. p660-p665.