2JSD

Solution structure of MMP20 complexed with NNGH

2JSD の概要

• エントリーDOI: 10.2210/pdb2jsd/pdb
• NMR情報: BMRB: 15361
• 分子名称: Matrix metalloproteinase-20, CALCIUM ION, ZINC ION, ... (4 entities in total)
• 機能のキーワード: mmp-nngh, structural genomics, structural proteomics in europe, spine, spine-2, spine2-complexes, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix (By similarity): O60882
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18023.83

構造登録者

Arendt, Y.,Banci, L.,Bertini, I.,Cantini, F.,Cozzi, R.,Del Conte, R.,Gonnelli, L.,Structural Proteomics in Europe (SPINE) (登録日: 2007-07-03, 公開日: 2007-11-20, 最終更新日: 2024-05-29)

主引用文献

Arendt, Y.,Banci, L.,Bertini, I.,Cantini, F.,Cozzi, R.,Del Conte, R.,Gonnelli, L.
Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase.
Febs Lett., 581:4723-4726, 2007

PubMed Abstract: The solution structure of the catalytic domain of MMP-20, a member of the matrix metalloproteinases family not yet structurally characterized, complexed with N-Isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid (NNGH), is here reported and compared with other MMPs-NNGH adducts. The backbone dynamic has been characterized as well. We have found that, despite the same fold and very high overall similarity, the present structure experiences specific structural and dynamical similarities with some MMPs and differences with others, around the catalytic cavity. The present solution structure, not only contributes to fill the gap of structural knowledge on human MMPs, but also provides further information to design more selective and efficient inhibitors for a specific member of this class of proteins.

PubMed: 17869250
DOI: 10.1016/j.febslet.2007.08.069

実験手法

SOLUTION NMR