1fzc
CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN WITH TWO DIFFERENT BOUND LIGANDS
OverviewOverview
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.
About this StructureAbout this Structure
1FZC is a Protein complex structure of sequences from Homo sapiens. The following page contains interesting information on the relation of 1FZC with [Fibrin]. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Fri May 2 16:56:06 2008