1YTV
Maltose-binding protein fusion to a C-terminal fragment of the V1a vasopressin receptor
Summary for 1YTV
Entry DOI | 10.2210/pdb1ytv/pdb |
Related | 1A7L |
Related PRD ID | PRD_900001 |
Descriptor | Maltose-binding periplasmic protein, Vasopressin V1a receptor, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (4 entities in total) |
Functional Keywords | vasopressin; receptor; gpcr; fusion protein; maltose-binding protein, sugar binding protein, hormone receptor |
Biological source | Escherichia coli More |
Cellular location | Cell membrane; Multi-pass membrane protein: P37288 |
Total number of polymer chains | 4 |
Total formula weight | 100314.29 |
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 citation | Adikesavan, 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: 16511036DOI: 10.1107/S1744309105007293 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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