1apo

THREE-DIMENSIONAL STRUCTURE OF THE APO FORM OF THE N-TERMINAL EGF-LIKE MODULE OF BLOOD COAGULATION FACTOR X AS DETERMINED BY NMR SPECTROSCOPY AND SIMULATED FOLDING

spinqualitylabelsall models 1apo, 13 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1apo is a 1 chain structure with sequence from Bovin. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: OH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FA10_BOVIN] Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. 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 The three-dimensional structure of a 42-residue fragment containing the N-terminal EGF-like module of blood coagulation factor X was determined by means of 2D NMR spectroscopy and computer simulation. The spectroscopic data consisted of 370 NOE distances and 27 dihedral angle constraints. These were used to generate peptide conformations by molecular dynamics simulation. The simulations used a novel functional form for the constraint potentials and were performed with two time steps to ensure rapid execution. Apart from preliminary runs to aid assignment of NOEs, 60 runs resulted in 13 accepted structures, which have two antiparallel beta sheets, no alpha helices, and five tight turns. There is no hydrophobic cluster. The root mean square deviation for the backbone of the 13 conformations is 0.65 +/- 0.11 A against their mean conformation. About half of the side chains have well-defined structure. The overall conformation is similar to that of murine EGF. Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding.,Ullner M, Selander M, Persson E, Stenflo J, Drakenberg T, Teleman O Biochemistry. 1992 Jul 7;31(26):5974-83. PMID:1627540 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Factor Xa

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