2JNP

Solution structure of matrix metalloproteinase 3 (MMP-3) in the presence of N-isobutyl-N-[4-methoxyphenylsulfonyl]glycyl hydroxamic acid (NNGH)

2JNP の概要

• エントリーDOI: 10.2210/pdb2jnp/pdb
• NMR情報: BMRB: 15120
• 分子名称: Matrix metalloproteinase-3, ZINC ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: metalloproteinase, mmp, hydrolase
• 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: 18570.38

構造登録者

Alcaraz, L.A.,Banci, L.,Bertini, I.,Cantini, F.,Donaire, A.,Gonnelli, L. (登録日: 2007-01-30, 公開日: 2007-12-11, 最終更新日: 2024-05-08)

主引用文献

Alcaraz, L.A.,Banci, L.,Bertini, I.,Cantini, F.,Donaire, A.,Gonnelli, L.
Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors
J.Biol.Inorg.Chem., 12:1197-1206, 2007

PubMed Abstract: We structurally characterized the adducts of the catalytic domain of matrix metalloproteinase-3 (MMP3) with three different nonpeptidic inhibitors by solving the solution structure of one adduct [MMP3-N-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid] and then by calculating structural models of the other two adducts using a reduced set of experimental NMR data, following a recently proposed procedure (Bertini et al. in J. Med. Chem. 48:7544-7559, 2005). The inhibitors were selected with the criteria of maintaining in all of them the same zinc-coordinating moiety and of selectively changing the substituents and/or the functional groups. The backbone dynamics on various time scales have been characterized as well. The comparison among these structures and with others previously reported allowed us to elucidate fine details of inhibitor-receptor interactions and to develop some criteria, which could guide in optimizing the design of selective inhibitors.

PubMed: 17710450
DOI: 10.1007/s00775-007-0288-9

実験手法

SOLUTION NMR