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 [[EFh domains|EFh domains]] which are responsible | There are four [[EFh domains|EFh domains]] which are responsible to bind 4 Ca2+<sup></sup> molecules<ref>http://smart.embl-heidelberg.de/smart/job_status.pl?jobid=939661123169621289746763YwAuDuwGQT</ref><br> | ||
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.<ref>John T.Hancock (2005).Cell signalling. New York:Oxford University press</ref><sup></sup> | |||
=== Function === | === Function === | ||
Revision as of 14:23, 25 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]
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.[4]
Function
Calmodulin binds Ca2+ to maintain low cytosolic Ca2+ concentration
Two or more Ca2+ ions bind to induce a conformational change and activate calmodulin [5]
References
- ↑ Alberts et al. Molecular Biology of the Cell (5th Ed)
- ↑ http://www.ncbi.nlm.nih.gov/protein/CAA36839.1
- ↑ http://smart.embl-heidelberg.de/smart/job_status.pl?jobid=939661123169621289746763YwAuDuwGQT
- ↑ John T.Hancock (2005).Cell signalling. New York:Oxford University press
- ↑ Alberts et al. Molecular Biology of the Cell (5th Ed)