2chd

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==Overview==
==Overview==
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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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?16790935 (full description)]]
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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==
==About this Structure==
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2CHD 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 GOL as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CHD OCA]].
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2CHD 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 GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CHD OCA].
==Reference==
==Reference==
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[[Category: zinc-finger]]
[[Category: zinc-finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:08:21 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:42:38 2007''

Revision as of 12:37, 5 November 2007


2chd, resolution 1.92Å

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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 with GOL as ligand. Structure known Active Site: AC1. 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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