3BA0

Crystal structure of full-length human MMP-12

3BA0 の概要

• エントリーDOI: 10.2210/pdb3ba0/pdb
• 関連するPDBエントリー: 1SU3
• 分子名称: Macrophage metalloelastase, ZINC ION, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: full-length mmp-12, hemopexin domain, catalytic domain, domain interaction., calcium, extracellular matrix, glycoprotein, hydrolase, metal-binding, metalloprotease, polymorphism, protease, secreted, zinc, zymogen
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42509.54

構造登録者

Bertini, I.,Calderone, V.,Fragai, M.,Jaiswal, R.,Luchinat, C.,Melikian, M.,Myonas, E.,Svergun, D.I. (登録日: 2007-11-07, 公開日: 2008-07-29, 最終更新日: 2024-10-30)

主引用文献

Bertini, I.,Calderone, V.,Fragai, M.,Jaiswal, R.,Luchinat, C.,Melikian, M.,Mylonas, E.,Svergun, D.I.
Evidence of reciprocal reorientation of the catalytic and hemopexin-like domains of full-length MMP-12.
J.Am.Chem.Soc., 130:7011-7021, 2008

PubMed Abstract: The proteolytic activity of matrix metalloproteinases toward extracellular matrix components (ECM), cytokines, chemokines, and membrane receptors is crucial for several homeostatic and pathological processes. Active MMPs are a family of single-chain enzymes (23 family members in the human genome), most of which constituted by a catalytic domain and by a hemopexin-like domain connected by a linker. The X-ray structures of MMP-1 and MMP-2 suggest a conserved and well-defined spatial relationship between the two domains. Here we present structural data for MMP-12, suitably stabilized against self-hydrolysis, both in solution (NMR and SAXS) and in the solid state (X-ray), showing that the hemopexin-like and the catalytic domains experience conformational freedom with respect to each other on a time scale shorter than 10(-8) s. Hints on the probable conformations are also obtained. This experimental finding opens new perspectives for the often hypothesized active role of the hemopexin-like domain in the enzymatic activity of MMPs.

PubMed: 18465858
DOI: 10.1021/ja710491y

実験手法

X-RAY DIFFRACTION (3 Å)