2dfk

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(New page: 200px<br /> <applet load="2dfk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dfk, resolution 2.15&Aring;" /> '''Crystal structure o...)
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Revision as of 19:25, 12 November 2007

Image:2dfk.gif

2dfk, resolution 2.15Å

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Crystal structure of the CDC42-Collybistin II complex

Overview

The synaptic localization of ion channel receptors is essential for, efficient synaptic transmission and the precise regulation of diverse, neuronal functions. In the central nervous system, ion channel receptors, reside in the postsynaptic membrane where they are juxtaposed to, presynaptic terminals. For proper function, these ion channels have to be, anchored to the cytoskeleton, and in the case of the inhibitory glycine, and gamma-amino-butyric acid type A (GABA(A)) receptors this interaction, is mediated by a gephyrin centered scaffold. Highlighting its central role, in this receptor anchoring scaffold, gephyrin interacts with a number of, proteins, including the neurospecific guanine nucleotide exchange factor, collybistin. Collybistin belongs to the Dbl family of guanine nucleotide, exchange factors, occurs in multiple splice variants, and is specific for, Cdc42, a small GTPase belonging to the Rho family. The 2.3 Angstroms, resolution crystal structure of the Cdc42-collybistin II complex reveals a, novel conformation of the switch I region of Cdc42. It also provides the, first direct observation of structural changes in the relative orientation, of the Dbl-homology domain and the pleckstrin-homology domain in the same, Dbl family protein. Biochemical data indicate that gephyrin negatively, regulates collybistin activity.

About this Structure

2DFK is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus with SO4 and GOL as ligands. Full crystallographic information is available from OCA.

Reference

The crystal structure of Cdc42 in complex with collybistin II, a gephyrin-interacting guanine nucleotide exchange factor., Xiang S, Kim EY, Connelly JJ, Nassar N, Kirsch J, Winking J, Schwarz G, Schindelin H, J Mol Biol. 2006 May 26;359(1):35-46. Epub 2006 Mar 29. PMID:16616186

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