1FZC

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

Summary for 1FZC

• Entry DOI: 10.2210/pdb1fzc/pdb
• Descriptor: FIBRIN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose, ... (10 entities in total)
• Functional Keywords: blood coagulation, plasma protein, crosslinking
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 10
• Total formula weight: 171315.78

Authors

Everse, S.J.,Spraggon, G.,Veerapandian, L.,Riley, M.,Doolittle, R.F. (deposition date: 1998-05-19, release date: 1998-10-14, Last modification date: 2024-04-03)

Primary citation

Everse, S.J.,Spraggon, G.,Veerapandian, L.,Riley, M.,Doolittle, R.F.
Crystal structure of fragment double-D from human fibrin with two different bound ligands.
Biochemistry, 37:8637-8642, 1998

PubMed Abstract: 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.

PubMed: 9628725
DOI: 10.1021/bi9804129

Experimental method

X-RAY DIFFRACTION (2.3 Å)