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    Biochemistry. 1998 Jun 16;37(24):8637-42.

    Crystal structure of fragment double-D from human fibrin with two different bound ligands.

    Everse SJ, Spraggon G, Veerapandian L, Riley M, Doolittle RF.

    Center for Molecular Genetics, University of California, San Diego, La Jolla, California 92093-0634, USA.

    Factor XIII-cross-linked fragment D (double-D) from human fibrin was crystallized in the presence of two different peptide ligands and the X-ray structure determined at 2.3 A. The peptide Gly-Pro-Arg-Pro-amide, which is an analogue of the knob exposed by the thrombin-catalyzed removal of fibrinopeptide A, was found to reside in the gamma-chain holes, and the peptide Gly-His-Arg-Pro-amide, which corresponds to the beta-chain knob, was found in the homologous beta-chain holes. The structure shows for the first time that the beta-chain knob does indeed bind to a homologous hole on the beta-chain. The gamma- and beta-chain holes are structurally very similar, and it is remarkable they are able to distinguish between these two peptides that differ by a single amino acid. Additionally, we have found that the beta-chain domain, like its gamma-chain counterpart, binds calcium.

    PMID: 9628725 [PubMed - indexed for MEDLINE]

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