A C-terminal segment of the V(1)R vasopressin receptor is unstructured in the crystal structure of its chimera with the maltose-binding protein. Export

@article{citeulike:531280, abstract = {The V(1) vascular vasopressin receptor (V(1)R) 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 V(1)R 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 V(1)R.}, address = {Department of Biochemistry, School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, OH 44106-4935, USA.}, author = {Adikesavan, N. V. and Mahmood, S. S. and Stanley, N. and Xu, Z. and Wu, N. and Thibonnier, M. and Shoham, M.}, citeulike-article-id = {531280}, citeulike-linkout-0 = {http://dx.doi.org/10.1107/S1744309105007293}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/16511036}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=16511036}, doi = {10.1107/S1744309105007293}, issn = {1744-3091}, journal = {Acta Crystallograph Sect F Struct Biol Cryst Commun}, keywords = {chimera, crystallography, cterm}, month = {April}, number = {Pt 4}, pages = {341--345}, posted-at = {2006-03-06 10:08:43}, priority = {1}, title = {A C-terminal segment of the V(1)R vasopressin receptor is unstructured in the crystal structure of its chimera with the maltose-binding protein.}, url = {http://dx.doi.org/10.1107/S1744309105007293}, volume = {61}, year = {2005} }

TY - JOUR ID - citeulike:531280 L3 - citeulike-article-id:531280 N2 - The V(1) vascular vasopressin receptor (V(1)R) 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 V(1)R 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 V(1)R. IS - Pt 4 JF - Acta Crystallograph Sect F Struct Biol Cryst Commun SN - 1744-3091 AD - Department of Biochemistry, School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, OH 44106-4935, USA. EP - 345 TI - A C-terminal segment of the V(1)R vasopressin receptor is unstructured in the crystal structure of its chimera with the maltose-binding protein. VL - 61 SP - 341 KW - chimera KW - crystallography KW - cterm AU - Adikesavan, NV AU - Mahmood, SS AU - Stanley, N AU - Xu, Z AU - Wu, N AU - Thibonnier, M AU - Shoham, M PY - 2005/04/01/ UR - http://dx.doi.org/10.1107/S1744309105007293 ER -