1CXW
THE SECOND TYPE II MODULE FROM HUMAN MATRIX METALLOPROTEINASE 2
1CXW の概要
| エントリーDOI | 10.2210/pdb1cxw/pdb |
| NMR情報 | BMRB: 4510 |
| 分子名称 | HUMAN MATRIX METALLOPROTEINASE 2 (1 entity in total) |
| 機能のキーワード | beta sheet, alpha helix, hydrolase |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Secreted, extracellular space, extracellular matrix: P08253 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 6773.36 |
| 構造登録者 | Briknarova, K.,Grishaev, A.,Banyai, L.,Tordai, H.,Patthy, L.,Llinas, M. (登録日: 1999-08-31, 公開日: 1999-11-12, 最終更新日: 2024-10-30) |
| 主引用文献 | Briknarova, K.,Grishaev, A.,Banyai, L.,Tordai, H.,Patthy, L.,Llinas, M. The second type II module from human matrix metalloproteinase 2: structure, function and dynamics. Structure Fold.Des., 7:1235-1245, 1999 Cited by PubMed Abstract: Matrix metalloproteinase 2 (MMP-2, gelatinase A, 72 kDa type IV collagenase) has an important role in extracellular matrix degradation during cell migration and tissue remodeling. It is involved in development, inflammation, wound healing, tumor invasion, metastasis and other physiological and pathological processes. The enzyme cleaves several types of collagen, elastin, fibronectin and laminin. Binding to collagen is mediated by three repeats homologous to fibronectin type II modules, which are inserted in the catalytic domain in proximity to the active site. PubMed: 10545322DOI: 10.1016/S0969-2126(00)80057-X 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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