2H43

Crystal Structure of Human Fragment D Complexed with Ala-His-Arg-Pro-amide

2H43 の概要

• エントリーDOI: 10.2210/pdb2h43/pdb
• 関連するPDBエントリー: 1FZG
• 分子名称: Fibrinogen alpha chain, Fibrinogen beta chain, Fibrinogen gamma chain, ... (7 entities in total)
• 機能のキーワード: knob-hole interaction, fragment d, coiled-coil, blood clotting
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 171051.43

構造登録者

Doolittle, R.F.,Pandi, L. (登録日: 2006-05-23, 公開日: 2006-12-05, 最終更新日: 2024-10-30)

主引用文献

Doolittle, R.F.,Chen, A.,Pandi, L.
Differences in Binding Specificity for the Homologous gamma- and beta-Chain "Holes" on Fibrinogen: Exclusive Binding of Ala-His-Arg-Pro-amide by the beta-Chain Hole.
Biochemistry, 45:13962-13969, 2006

PubMed Abstract: The beta-chain amino-terminal sequences of all known mammalian fibrins begin with the sequence Gly-His-Arg-Pro- (GHRP-), but the homologous sequence in chicken fibrin begins with the sequence Ala-His-Arg-Pro- (AHRP-). Nonetheless, chicken fibrinogen binds the synthetic peptide GHRPam, and a previously reported crystal structure has revealed that the binding is in exact conformance with that observed for the human GHRPam-fragment D complex. We now report that human fibrinogen, which is known not to bind APRP, binds the synthetic peptide AHRPam. Moreover, a crystal structure of AHRPam complexed with fragment D from human fibrinogen shows that AHRPam binds exclusively to the beta-chain hole and, unlike GHRPam, not at all to the homologous gamma-chain hole. The difference can be attributed to the methyl group of the alanine residue clashing with a critical carboxyl group in the gammaC hole but being accommodated in the roomier betaC hole where the equivalent carboxyl is situated more flexibly.

PubMed: 17115691
DOI: 10.1021/bi061219e

実験手法

X-RAY DIFFRACTION (2.7 Å)