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1ytv

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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])
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|DOMAIN=
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|RELATEDENTRY=[[1a7l|1A7L]]
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|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.]]
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[[Category: MAL]]
+
[[Category: fusion protein]]
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[[Category: vasopressin; receptor; gpcr; fusion protein; maltose-binding protein]]
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[[Category: gpcr]]
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[[Category: maltose-binding protein]]
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[[Category: receptor]]
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[[Category: vasopressin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:27:28 2008''
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''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


PDB ID 1ytv

Drag the structure with the mouse to rotate
, resolution 1.80Å
Ligands:
Gene: malE (Escherichia coli), AVPR1A (Homo sapiens)
Related: 1A7L


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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