2DOI

The X-ray crystallographic structure of the angiogenesis inhibitor, angiostatin, bound to a peptide from the group A streptococcus protein PAM

2DOI の概要

• エントリーDOI: 10.2210/pdb2doi/pdb
• 関連するPDBエントリー: 2DOH
• 分子名称: Angiostatin, Plasminogen-binding group A streptococcal M-like protein PAM (2 entities in total)
• 機能のキーワード: plasminogen, kringle domain, lysine-binding site, pseudo-lysine moiety, hydrolase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Secreted : P00747; Secreted, cell wall ; Peptidoglycan-anchor : P49054
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 60785.28

構造登録者

Cnudde, S.E.,Prorok, M.,Castellino, F.J.,Geiger, J.H. (登録日: 2006-04-29, 公開日: 2006-12-05, 最終更新日: 2024-10-16)

主引用文献

Cnudde, S.E.,Prorok, M.,Castellino, F.J.,Geiger, J.H.
X-ray crystallographic structure of the angiogenesis inhibitor, angiostatin, bound to a peptide from the group A streptococcal surface protein PAM
Biochemistry, 45:11052-11060, 2006

PubMed Abstract: The crystal structure of the human Pg-derived angiogenesis inhibitor, angiostatin, complexed to VEK-30, a peptide from the group A streptococcal surface protein, PAM, was determined and refined to 2.3 A resolution. This is the first structure of angiostatin bound to a ligand and provides a model of the interaction between Pg and streptococcal-derived pathogenic proteins. VEK-30 contains a "through-space isostere" for C-terminal lysine, wherein Arg and Glu side chains, separated by one helical turn, bind within the bipolar angiostatin kringle 2 (K2) domain lysine-binding site. VEK-30 also makes several contacts with K2 residues that exist outside of the canonical LBS and are not conserved among the other Pg kringles, thus providing a molecular basis for the selectivity of VEK-30 for K2. The structure also shows that Pg kringle domains undergo significant structural rearrangement relative to one another and reveals dimerization between two molecules of angiostatin and VEK-30 related by crystallographic symmetry. This dimerization, which exists only in the crystal structure, is consistent with the parallel coiled-coil full-length PAM dimer expected from sequence similarities and homology modeling.

PubMed: 16964966
DOI: 10.1021/bi060914j

実験手法

X-RAY DIFFRACTION (3.1 Å)