1ytv: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= malE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), AVPR1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= malE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), AVPR1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1a7l|1A7L]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ytv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ytv OCA], [http://www.ebi.ac.uk/pdbsum/1ytv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ytv RCSB]</span> | |||
}} | }} | ||
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[[Category: Wu, N.]] | [[Category: Wu, N.]] | ||
[[Category: Xu, Z.]] | [[Category: Xu, Z.]] | ||
[[Category: | [[Category: fusion protein]] | ||
[[Category: | [[Category: gpcr]] | ||
[[Category: maltose-binding protein]] | |||
[[Category: receptor]] | |||
[[Category: vasopressin]] | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:22:06 2008'' | ||
Revision as of 22:22, 30 March 2008
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| 1ytv, resolution 1.80Å | |||||||||||||
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| Ligands: | MAL | ||||||||||||
| Gene: | malE (Escherichia coli), AVPR1A (Homo sapiens) | ||||||||||||
| Related: | 1A7L
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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 Crystallogr Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt, 4):341-5. Epub 2005 Mar 24. PMID:16511036
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