6ebx

STRUCTURE DETERMINATION OF A DIMERIC FORM OF ERABUTOXIN B, CRYSTALLIZED FROM THIOCYANATE SOLUTION

spinqualitylabelsall models 6ebx, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ebx is a 2 chain structure with sequence from Laticauda semifasciata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SCN Resources: FirstGlance, OCA, RCSB, PDBsum Function [NXSB_LATSE] Binds with high affinity to muscular nicotinic acetylcholine receptors (nAChRs), and with low affinity to neuronal alpha-7 nAChRs. Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Erabutoxin-b, M(r) = 6861.1, a single 62 amino-acid chain folded by four disulfide bridges, was crystallized in a new orthorhombic form by using thiocyanate as crystallizing agent. The space group is P2(1)2(1)2(1) with a = 53.36 (4), b = 40.89 (4), c = 55.71 (5) A, V = 121533.1 A and Z = 8. X-ray diffraction data were recorded at the LURE synchrotron facility (lambda = 1.405 A). The structure was solved by molecular replacement and shows a dimeric association through an anti-parallel beta-sheet around the twofold non-crystallographic axis. The two independent molecules, one SCN- ion and 97 associated water molecules were refined by molecular dynamics and annealing techniques to R = 19.6% (10,913 Fobs, resolution 5-1.7 A). The thiocyanate ion is located at the interface of the dimer and close to the non-crystallographic twofold axis. Structure determination of a dimeric form of erabutoxin-b, crystallized from a thiocyanate solution.,Saludjian P, Prange T, Navaza J, Menez R, Guilloteau JP, Ries-Kautt M, Ducruix A Acta Crystallogr B. 1992 Aug 1;48 ( Pt 4):520-31. PMID:1418823 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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