1t3l
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(New page: 200px<br /><applet load="1t3l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t3l, resolution 2.20Å" /> '''Structural Analysis ...)
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Revision as of 00:50, 21 November 2007
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Structural Analysis of the Voltage-Dependent Calcium Channel Beta Subunit Functional Core in Complex with Alpha1 Interaction Domain
Overview
Voltage-dependent calcium channels (VDCC) are multiprotein assemblies that, regulate the entry of extracellular calcium into electrically excitable, cells and serve as signal transduction centers. The alpha1 subunit forms, the membrane pore while the intracellular beta subunit is responsible for, trafficking of the channel to the plasma membrane and modulation of its, electrophysiological properties. Crystallographic analyses of a beta, subunit functional core alone and in complex with a alpha1 interaction, domain (AID) peptide, the primary binding site of beta to the alpha1, subunit, reveal that beta represents a novel member of the MAGUK protein, family. The findings illustrate how the guanylate kinase fold has been, fashioned into a protein-protein interaction module by alteration of one, of its substrate sites. Combined results indicate that the AID peptide, undergoes a helical transition in binding to beta. We outline the, mechanistic implications for understanding the beta subunit's broad, regulatory role of the VDCC, particularly via the AID.
About this Structure
1T3L is a Protein complex structure of sequences from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
Structural analysis of the voltage-dependent calcium channel beta subunit functional core and its complex with the alpha 1 interaction domain., Opatowsky Y, Chen CC, Campbell KP, Hirsch JA, Neuron. 2004 May 13;42(3):387-99. PMID:15134636
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