2chd
From Proteopedia
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| - | [[Image:2chd.gif|left|200px]] | + | [[Image:2chd.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE C2A DOMAIN OF RABPHILIN-3A''' | + | {{Structure |
| + | |PDB= 2chd |SIZE=350|CAPTION= <scene name='initialview01'>2chd</scene>, resolution 1.92Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE C2A DOMAIN OF RABPHILIN-3A''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CHD is a [ | + | 2CHD 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=2CHD OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the C2A domain of rabphilin-3A., Biadene M, Montaville P, Sheldrick GM, Becker S, Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):793-9. Epub 2006, Jun 20. PMID:[http:// | + | Structure of the C2A domain of rabphilin-3A., Biadene M, Montaville P, Sheldrick GM, Becker S, Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):793-9. Epub 2006, Jun 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16790935 16790935] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
| - | ''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 16:15:22 2008'' |
Revision as of 14:15, 20 March 2008
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| , resolution 1.92Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE C2A DOMAIN OF RABPHILIN-3A
Overview
Rabphilin-3A is a neuronal protein containing a C2-domain tandem. To date, only the structure of the C2B domain has been solved. The crystal structure of the Ca2+-free C2A domain has been solved by molecular replacement and refined to 1.92 A resolution. It adopts the classical C2-domain fold consisting of an eight-stranded antiparallel beta-sandwich with type I topology. In agreement with its Ca2+-dependent negatively charged membrane-binding properties, this C2 domain contains all the conserved acidic residues responsible for calcium binding. However, the replacement of a conserved aspartic acid residue by glutamic acid allows formation of an additional strong hydrogen bond, resulting in increased rigidity of calcium-binding loop 1. The electrostatic surface of the C2A domain consists of a large positively charged belt surrounded by two negatively charged patches located at both tips of the domain. In comparison, the structurally very similar C2A domain of synaptotagmin I has a highly acidic electrostatic surface, suggesting completely unrelated functions for these two C2A domains.
About this Structure
2CHD is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure of the C2A domain of rabphilin-3A., Biadene M, Montaville P, Sheldrick GM, Becker S, Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):793-9. Epub 2006, Jun 20. PMID:16790935
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