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PH domain

2011-11-25T01:55:01Z

100501805:

A Pleckstrin Homology domain or PH Domain is a protein composed of around 100 amino acids that is found within numerous protein families involved with intracellular signalling<ref>Mussacchio A, Gibson T, Rice P, Thompson J, Saraste M. 1993 The PH Domain: a Common Piece in the Structural Patchwork of Siganlling Proteins. Trends in Biochemical Sciences [e-journal] 18(9): 343-8</ref>. Originally found in Pleckstrin <ref>Mayer B.J, Ren R., Clark K.L., Baltimore D., 1993 A Putative Modular Domain Present in Diverse Signalling Proteins. ''Cell ''[e-journal] 73(4): 629-630</ref> it has since been detected in around 200 human proteins<ref>Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P, 2008. Molecular Biology of the Cell, 5th Edition. New York: Garland Science. p933</ref> as well as other eukaryotic proteins. The primary function of the domain appears to be the binding of inositol phosphates though other related proteins are also able to bind.

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The structure though varying to some degree depending on which domains the PH domain is within, certain features are conserved. These are the presence of a C-terminal alpha helix closely associated with a beta sheet consisting of 7 strands.<ref>Saraste M, Hyvönen M, 1995. Pleckstrin homology domains: a fact file. ''Current Opinions in Structural Biology'', [e-journal] 5(3): 403-8.</ref>

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PH domain

2011-11-25T01:54:40Z

100501805:

A Pleckstrin Homology domain or PH Domain is a protein composed of around 100 amino acids that is found within numerous protein families involved with intracellular signalling<ref>Mussacchio A, Gibson T, Rice P, Thompson J, Saraste M. 1993 The PH Domain: a Common Piece in the Structural Patchwork of Siganlling Proteins. Trends in Biochemical Sciences [e-journal] 18(9): 343-8</ref>. Originally found in Pleckstrin <ref>Mayer B.J, Ren R., Clark K.L., Baltimore D., 1993 A Putative Modular Domain Present in Diverse Signalling Proteins. ''Cell ''[e-journal] 73(4): 629-630</ref> it has since been detected in around 200 human proteins<ref>Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P, 2008. Molecular Biology of the Cell, 5th Edition. New York: Garland Science. p933</ref> as well as other eukaryotic proteins. The primary function of the domain appears to be the binding of inositol phosphates though other related proteins are also able to bind.

The structure though varying to some degree depending on which domains the PH domain is within, certain features are conserved. These are the presence of a C-terminal alpha helix closely associated with a beta sheet consisting of 7 strands.<ref>Saraste M, Hyvönen M, 1995. Pleckstrin homology domains: a fact file. ''Current Opinions in Structural Biology'', [e-journal] 5(3): 403-8.</ref><references />

PH domain

2011-11-25T01:54:13Z

100501805:

A Pleckstrin Homology domain or PH Domain is a protein composed of around 100 amino acids that is found within numerous protein families involved with intracellular signalling<ref>Mussacchio A, Gibson T, Rice P, Thompson J, Saraste M. 1993 The PH Domain: a Common Piece in the Structural Patchwork of Siganlling Proteins. Trends in Biochemical Sciences [e-journal] 18(9): 343-8</ref>. Originally found in Pleckstrin <ref>Mayer B.J, Ren R., Clark K.L., Baltimore D., 1993 A Putative Modular Domain Present in Diverse Signalling Proteins. ''Cell ''[e-journal] 73(4): 629-630</ref> it has since been detected in around 200 human proteins<ref>Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P, 2008. Molecular Biology of the Cell, 5th Edition. New York: Garland Science. p933</ref> as well as other eukaryotic proteins. The primary function of the domain appears to be the binding of inositol phosphates though other related proteins are also able to bind. The structure though varying to some degree depending on which domains the PH domain is within, certain features are conserved. These are the presence of a C-terminal alpha helix closely associated with a beta sheet consisting of 7 strands.<ref>Saraste M, Hyvönen M, 1995. Pleckstrin homology domains: a fact file. ''Current Opinions in Structural Biology'', [e-journal] 5(3): 403-8.</ref><references />

PH domain

2011-11-25T01:48:07Z

100501805:

A Pleckstrin Homology domain or PH Domain is a protein composed of around 100 amino acids that is found within numerous protein families involved with intracellular signalling. Originally found in Pleckstrin <ref>Mayer B.J, Ren R., Clark K.L., Baltimore D., A Putative Modular Domain Present in Diverse Signalling Proteins. ''Cell ''[e-journal] 73(4): 629-630</ref> it has since been detected in around 200 human proteins<ref>Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P, 2008. Molecular Biology of the Cell, 5th Edition. New York: Garland Science. p933</ref> as well as other eukaryotic proteins. The primary function of the domain appears to be the binding of inositol phosphates though other related proteins are also able to bind. The structure though varying to some degree depending on which domains the PH domain is within, certain features are conserved. These are the presence of a C-terminal alpha helix closely associated with a beta sheet consisting of 7 strands.<ref>Saraste M, Hyvönen M, 1995. Pleckstrin homology domains: a fact file. ''Current Opinions in Structural Biology'', [e-journal] 5(3): 403-8.</ref><references />

PH domain

2011-11-25T01:45:43Z

100501805: Created page with "A Pleckstrin Homology domain or PH Domain is a protein composed of around 100 amino acids that is found within numerous protein families involved with intracellular signalling. O..."

A Pleckstrin Homology domain or PH Domain is a protein composed of around 100 amino acids that is found within numerous protein families involved with intracellular signalling. Originally found in Pleckstrin  <ref>Mayer B.J, Ren R., Clark K.L., Baltimore D., A Putative Modular Domain Present in Diverse Signalling Proteins. ''Cell ''[e-journal] 73(4): 629-630</ref> it has since been detected in around 200 human proteins<ref>Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P, 2008. Molecular Biology of the Cell, 5th Edition. New York: Garland Science.</ref> as well as other eukaryotic proteins. The primary function of the domain appears to be the binding of inositol phosphates though other related proteins are also able to bind.

The structure though varying to some degree depending on which domains the PH domain is within, certain features are conserved. These are the presence of a C-terminal alpha helix closely associated with a beta sheet consisting of 7 strands.<ref>Saraste M, Hyvönen M, 1995. Pleckstrin homology domains: a fact file. ''Current Opinions in Structural Biology'', [e-journal] 5(3): 403-8.</ref><references />

Promoter

2011-01-11T05:07:46Z

100501805: Created page with 'A promoter site is a region of DNA that RNA polymerase binds to in order to carry out transcription. It is located upstream of the target sequence. <ref>Biochemistry, 6th Ed…'

A promoter site is a region of DNA that RNA polymerase binds to in order to carry out transcription. It is located upstream of the target sequence. <ref>Biochemistry, 6th Edition, Jeremy M. Berg, John L. Tymoczko, Lubert Stryer, W. H. Freeman and Company, New York, 2008</ref><references />