2f2p

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[[Image:2f2p.gif|left|200px]]
[[Image:2f2p.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_2f2p", creates the "Structure Box" on the page.
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{{STRUCTURE_2f2p| PDB=2f2p | SCENE= }}
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|RELATEDENTRY=[[2f2o|2F2O]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f2p OCA], [http://www.ebi.ac.uk/pdbsum/2f2p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f2p RCSB]</span>
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'''Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode'''
'''Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode'''
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[[Category: Wong, A.]]
[[Category: Wong, A.]]
[[Category: Ye, Q.]]
[[Category: Ye, Q.]]
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[[Category: calcineurin]]
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[[Category: Calcineurin]]
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[[Category: calcium]]
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[[Category: Calcium]]
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[[Category: calmodulin]]
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[[Category: Calmodulin]]
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[[Category: ef-hand]]
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[[Category: Ef-hand]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:23:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:57:06 2008''
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Revision as of 00:23, 4 May 2008

Image:2f2p.gif

Template:STRUCTURE 2f2p

Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode


Overview

Calcineurin is a calmodulin-binding protein in brain and the only serine/threonine protein phosphatase under the control of Ca2+/calmodulin (CaM), which plays a critical role in coupling Ca2+ signals to cellular responses. CaM up-regulates the phosphatase activity of calcineurin by binding to the CaM-binding domain (CBD) of calcineurin subunit A. Here, we report crystal structural studies of CaM bound to a CBD peptide. The chimeric protein containing CaM and the CBD peptide forms an intimate homodimer, in which CaM displays a native-like extended conformation and the CBD peptide shows alpha-helical structure. Unexpectedly, the N-terminal lobe from one CaM and the C-terminal lobe from the second molecule form a combined binding site to trap the peptide. Thus, the dimer provides two binding sites, each of which is reminiscent of the fully collapsed conformation of CaM commonly observed in complex with, for example, the myosin light chain kinase (MLCK) peptide. The interaction between the peptide and CaM is highly specific and similar to MLCK.

About this Structure

2F2P is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode., Ye Q, Li X, Wong A, Wei Q, Jia Z, Biochemistry. 2006 Jan 24;45(3):738-45. PMID:16411749 Page seeded by OCA on Sun May 4 03:23:42 2008

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