1fzc

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1fzc, resolution 2.3Å

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CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN WITH TWO DIFFERENT BOUND LIGANDS

Contents

Overview

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.

Disease

Known diseases associated with this structure: Afibrinogenemia, congenital OMIM:[134820], Afibrinogenemia, congenital OMIM:[134830], Amyloidosis, hereditary renal OMIM:[134820], Dysfibrinogenemia, alpha type, causing bleeding diathesis OMIM:[134820], Dysfibrinogenemia, alpha type, causing recurrent thrombosis OMIM:[134820], Dysfibrinogenemia, beta type OMIM:[134830], Dysfibrinogenemia, gamma type OMIM:[134850], Hypofibrinogenemia, gamma type OMIM:[134850], Thrombophilia, dysfibrinogenemic OMIM:[134830], Thrombophilia, dysfibrinogenemic OMIM:[134850]

About this Structure

1FZC is a Protein complex structure of sequences from Homo sapiens with NAG, MAN and CA as ligands. The following page contains interesting information on the relation of 1FZC with [Fibrin]. Full crystallographic information is available from OCA.

Reference

Crystal structure of fragment double-D from human fibrin with two different bound ligands., Everse SJ, Spraggon G, Veerapandian L, Riley M, Doolittle RF, Biochemistry. 1998 Jun 16;37(24):8637-42. PMID:9628725

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