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1YTV

Maltose-binding protein fusion to a C-terminal fragment of the V1a vasopressin receptor

Summary for 1YTV
Entry DOI10.2210/pdb1ytv/pdb
Related1A7L
Related PRD IDPRD_900001
DescriptorMaltose-binding periplasmic protein, Vasopressin V1a receptor, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (4 entities in total)
Functional Keywordsvasopressin; receptor; gpcr; fusion protein; maltose-binding protein, sugar binding protein, hormone receptor
Biological sourceEscherichia coli
More
Cellular locationCell membrane; Multi-pass membrane protein: P37288
Total number of polymer chains4
Total formula weight100314.29
Authors
Adikesavan, N.V.,Mahmood, S.S.,Stanley, S.,Xu, Z.,Wu, N.,Thibonnier, M.,Shoham, M. (deposition date: 2005-02-11, release date: 2005-04-12, Last modification date: 2023-09-20)
Primary citationAdikesavan, N.V.,Mahmood, S.S.,Stanley, N.,Xu, Z.,Wu, N.,Thibonnier, M.,Shoham, M.
A C-terminal segment of the V1R vasopressin receptor is unstructured in the crystal structure of its chimera with the maltose-binding protein.
Acta Crystallogr.,Sect.F, 61:341-345, 2005
Cited by
PubMed Abstract: 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.
PubMed: 16511036
DOI: 10.1107/S1744309105007293
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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