2ct9
From Proteopedia
(New page: 200px<br /><applet load="2ct9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ct9, resolution 2.20Å" /> '''The crystal structur...) |
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| - | [[Image:2ct9.gif|left|200px]]<br /><applet load="2ct9" size=" | + | [[Image:2ct9.gif|left|200px]]<br /><applet load="2ct9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ct9, resolution 2.20Å" /> | caption="2ct9, resolution 2.20Å" /> | ||
'''The crystal structure of calcineurin B homologous proein 1 (CHP1)'''<br /> | '''The crystal structure of calcineurin B homologous proein 1 (CHP1)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Calcineurin B homologous protein 1 (CHP1), also known as p22, is a | + | 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== | ==About this Structure== | ||
| - | 2CT9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2CT9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CT9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ef-hand]] | [[Category: ef-hand]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:52:11 2008'' |
Revision as of 14:52, 21 February 2008
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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 with as ligand. 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
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