Calmodulin: Difference between revisions

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Highly conserved sequence of 152 [[Amino acids|amino acids]] <ref>http://www.ncbi.nlm.nih.gov/protein/CAA36839.1</ref>  
Highly conserved sequence of 152 [[Amino acids|amino acids]] <ref>http://www.ncbi.nlm.nih.gov/protein/CAA36839.1</ref>  


There are four&nbsp;[[EFh domains|EFh domains]] which are responsible to bind 4 Ca<sup>2+</sup><sup></sup>&nbsp; molecules<ref>http://smart.embl-heidelberg.de/smart/job_status.pl?jobid=939661123169621289746763YwAuDuwGQT</ref><br>  
There are four&nbsp;[[EFh domains|EFh domains]] which are responsible to bind 4 Ca<sup>2+</sup><sup></sup>&nbsp; molecules<ref>http://smart.embl-heidelberg.de/smart/job_status.pl?jobid=939661123169621289746763YwAuDuwGQT</ref>&nbsp;<br>  


Calmodulin are dumbbell shaped protein where long and flexible [[Alpha-helix|alpha helix]] connects two [[globular domains|globular domains]]. Each domain is assembled from two [[EF-hand|EF-hand]] regions attached to antiparalel [[beta-sheet|beta-sheet]]. Ca<sup>2+</sup> binds to [[glutamate|glutamate]] and [[aspartate|aspartate]] residues placed in the loop of EF-hand.<ref>John T.Hancock (2005).Cell signalling. New York:Oxford University press</ref><sup></sup>  
The arrangement of the Ca2+ binding sites are brought about by the N- and C- terminal lobes.<ref>http://www.cell-signalling.org/csb/004/csb004.pdf</ref>
 
Calmodulin are dumbbell shaped protein where long and flexible [[Alpha-helix|alpha helix]] connects two [[Globular domains|globular domains]]. Each domain is assembled from two [[EF-hand|EF-hand]] regions attached to antiparalel [[Beta-sheet|beta-sheet]]. Ca<sup>2+</sup> binds to [[Glutamate|glutamate]] and [[Aspartate|aspartate]] residues placed in the loop of EF-hand.<ref>John T.Hancock (2005).Cell signalling. New York:Oxford University press</ref><sup></sup>


=== Function  ===
=== Function  ===

Revision as of 16:22, 28 November 2011

Calcium binding protein involved in intracellular calcium signalling. [1]

Structure

Highly conserved sequence of 152 amino acids [2]

There are four EFh domains which are responsible to bind 4 Ca2+  molecules[3] 

The arrangement of the Ca2+ binding sites are brought about by the N- and C- terminal lobes.[4]

Calmodulin are dumbbell shaped protein where long and flexible alpha helix connects two globular domains. Each domain is assembled from two EF-hand regions attached to antiparalel beta-sheet. Ca2+ binds to glutamate and aspartate residues placed in the loop of EF-hand.[5]

Function

Calmodulin functions as a multi-purpose intracellular receptor,governing many Ca2+  regulated processes. [6] 

Two or more Ca2+ ions bind to induce a conformational change and activate calmodulin [7].

References

  1. Alberts et al. Molecular Biology of the Cell (5th Ed)
  2. http://www.ncbi.nlm.nih.gov/protein/CAA36839.1
  3. http://smart.embl-heidelberg.de/smart/job_status.pl?jobid=939661123169621289746763YwAuDuwGQT
  4. http://www.cell-signalling.org/csb/004/csb004.pdf
  5. John T.Hancock (2005).Cell signalling. New York:Oxford University press
  6. Alberts et al. Molecular Biology of the Cell (5th Ed).
  7. Alberts et al. Molecular Biology of the Cell (5th Ed)