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

Summary for 1APO

• Entry DOI: 10.2210/pdb1apo/pdb
• Descriptor: EGF-LIKE MODULE OF BLOOD COAGULATION FACTOR X, HYDROXIDE ION (2 entities in total)
• Functional Keywords: coagulation factor
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted: P00743
• Total number of polymer chains: 1
• Total formula weight: 4577.96

Authors

Ullner, M.,Selander, M.,Persson, E.,Stenflo, J.,Drakenberg, T.,Teleman, O. (deposition date: 1992-04-21, release date: 1994-01-31, Last modification date: 2017-11-29)

Primary citation

Ullner, M.,Selander, M.,Persson, E.,Stenflo, J.,Drakenberg, T.,Teleman, O.
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.
Biochemistry, 31:5974-5983, 1992

PubMed Abstract: 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.

PubMed: 1627540
DOI: 10.1021/bi00141a004

Experimental method

SOLUTION NMR