1ytv
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(New page: 200px<br /> <applet load="1ytv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ytv, resolution 1.80Å" /> '''Maltose-binding pro...)
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Revision as of 18:18, 12 November 2007
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Maltose-binding protein fusion to a C-terminal fragment of the V1a vasopressin receptor
Overview
The V1 vascular vasopressin receptor (V1R) is a G-protein-coupled receptor, (GPCR) involved in the regulation of body-fluid osmolality, blood volume, and blood pressure. Signal transduction is mediated by the third, intracellular loop of this seven-transmembrane protein as well as by the, C-terminal cytoplasmic segment. A chimera of the maltose-binding protein, (MBP) and the C-terminal segment of V1R has been cloned, expressed, purified and crystallized. The crystals belong to space group P2(1), with, unit-cell parameters a = 51.10, b = 66.56, c = 115.72 A, beta = 95.99, degrees. The 1.8 A crystal structure reveals the conformation of MBP and, part of the linker region of this chimera, with the C-terminal segment, being unstructured. This may reflect a conformational plasticity in the, C-terminal segment that may be necessary for proper function of V1R.
About this Structure
1YTV is a Protein complex structure of sequences from Escherichia coli and Homo sapiens with MAL as ligand. Full crystallographic information is available from OCA.
Reference
A C-terminal segment of the V1R vasopressin receptor is unstructured in the crystal structure of its chimera with the maltose-binding protein., Adikesavan NV, Mahmood SS, Stanley N, Xu Z, Wu N, Thibonnier M, Shoham M, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt, 4):341-5. Epub 2005 Mar 24. PMID:16511036
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