1rhp

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spinqualitylabelsall models 1rhp, resolution 2.4Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF RECOMBINANT HUMAN PLATELET FACTOR 4

Overview

The crystal structure of human platelet factor 4 (PF4) has been solved to, a resolution of 2.4 A by molecular replacement and refined to an R-factor, of 24.1%. The structure consists of four polypeptide chains which form a, tetrameric unit. N-terminal residues, previously defined as a random coil, or extended loop region, form antiparallel beta-sheet-like structures that, form noncovalent associations between dimers. These antiparallel, beta-sheet-like structures are positioned lateral to the beta-bilayer, motif and stabilize the tetrameric unit. A positively charged ring of, lysine and arginine side chains encircles the PF4 tetramer sphere, presenting multiple potential sites and orientations for heparin binding., The electrostatic interactions of multiply charged amino acid side chains, and hydrogen bonding interactions at the AB/CD dimer interface serve to, stabilize the tetrameric structure further.

About this Structure

1RHP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of recombinant human platelet factor 4., Zhang X, Chen L, Bancroft DP, Lai CK, Maione TE, Biochemistry. 1994 Jul 12;33(27):8361-6. PMID:8031770

Page seeded by OCA on Mon Nov 12 19:03:59 2007