2ct9
From Proteopedia
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| - | [[Image:2ct9.gif|left|200px]] | + | [[Image:2ct9.gif|left|200px]] |
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| - | '''The crystal structure of calcineurin B homologous proein 1 (CHP1)''' | + | {{Structure |
| + | |PDB= 2ct9 |SIZE=350|CAPTION= <scene name='initialview01'>2ct9</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''The crystal structure of calcineurin B homologous proein 1 (CHP1)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CT9 is a [ | + | 2CT9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CT9 OCA]. |
==Reference== | ==Reference== | ||
| - | Structural characterization of calcineurin B homologous protein 1., Naoe Y, Arita K, Hashimoto H, Kanazawa H, Sato M, Shimizu T, J Biol Chem. 2005 Sep 16;280(37):32372-8. Epub 2005 Jun 29. PMID:[http:// | + | Structural characterization of calcineurin B homologous protein 1., Naoe Y, Arita K, Hashimoto H, Kanazawa H, Sato M, Shimizu T, J Biol Chem. 2005 Sep 16;280(37):32372-8. Epub 2005 Jun 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15987692 15987692] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ef-hand]] | [[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 16:19:35 2008'' |
Revision as of 14:19, 20 March 2008
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| , resolution 2.20Å | |||||||
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| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The crystal structure of calcineurin B homologous proein 1 (CHP1)
Overview
Calcineurin B homologous protein 1 (CHP1), also known as p22, is a calcium-binding EF-hand protein that plays a role in membrane trafficking. It binds to multiple effector proteins, including Na(+)/H(+) exchangers, a serine/threonine kinase, and calcineurin, potentially modulating their function. The crystal structure of calcium-bound CHP1 from rat has been determined at 2.2 Angstroms of resolution. The molecule has a compact alpha-helical structure containing four EF-hands. The overall folding topology of the protein is similar to that of the regulatory B subunit of calcineurin and to that of calcium- and integrin-binding protein. The calcium ion is coordinated in typical fashion in the third and fourth EF-hands, but the first and second EF-hands contain no calcium ion. The first EF-hand is maintained by internal interactions, and the second EF-hand is stabilized by hydrophobic interactions. CHP1 contains a hydrophobic pocket on the opposite side of the protein to the EF-hands that has been implicated in ligand binding.
About this Structure
2CT9 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structural characterization of calcineurin B homologous protein 1., Naoe Y, Arita K, Hashimoto H, Kanazawa H, Sato M, Shimizu T, J Biol Chem. 2005 Sep 16;280(37):32372-8. Epub 2005 Jun 29. PMID:15987692
Page seeded by OCA on Thu Mar 20 16:19:35 2008
