2f2p
From Proteopedia
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| - | [[Image:2f2p.gif|left|200px]] | + | [[Image:2f2p.gif|left|200px]] |
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| - | '''Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode''' | + | {{Structure |
| + | |PDB= 2f2p |SIZE=350|CAPTION= <scene name='initialview01'>2f2p</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2F2P is a [ | + | 2F2P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F2P OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16411749 16411749] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: calcium]] | [[Category: calcium]] | ||
[[Category: calmodulin]] | [[Category: calmodulin]] | ||
| - | [[Category: ef- | + | [[Category: ef-hand]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:47:21 2008'' |
Revision as of 14:47, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 16:47:21 2008
Categories: Bos taurus | Single protein | Jia, Z. | Wong, A. | Ye, Q. | CA | Calcineurin | Calcium | Calmodulin | Ef-hand
