3SHI

Crystal structure of human MMP1 catalytic domain at 2.2 A resolution

3SHI の概要

• エントリーDOI: 10.2210/pdb3shi/pdb
• 関連するPDBエントリー: 1CGE 1HFC 966C
• 分子名称: Interstitial collagenase, ZINC ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: matrix metalloproteinase, paramagnetic restraints, paramagnetic tag, lanthanides, protein refinement, residual dipolar couplings, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix : P03956
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 53127.11

構造登録者

Bertini, I.,Calderone, V.,Cerofolini, L.,Fragai, M.,Geraldes, C.F.G.C.,Hermann, P.,Luchinat, C.,Parigi, G.,Teixeira, J. (登録日: 2011-06-16, 公開日: 2011-09-21, 最終更新日: 2023-09-13)

主引用文献

Bertini, I.,Calderone, V.,Cerofolini, L.,Fragai, M.,Geraldes, C.F.,Hermann, P.,Luchinat, C.,Parigi, G.,Teixeira, J.M.
The catalytic domain of MMP-1 studied through tagged lanthanides.
Febs Lett., 586:557-567, 2012

PubMed Abstract: Pseudocontact shifts (pcs) and paramagnetic residual dipolar couplings (rdc) provide structural information that can be used to assess the adequacy of a crystallographic structure to represent the solution structure of a protein. This can be done by attaching a lanthanide binding tag to the protein. There are cases in which only local rearrangements are sufficient to match the NMR data and cases where significant secondary structure or domain rearrangements from the solid state to the solution state are needed. We show that the two cases are easily distinguishable. Whereas the use of solution restraints in the latter case is described in the literature, here we deal with how to obtain a better model of the solution structure in a case (the catalytic domain of the matrix metalloproteinase MMP-1) of the former class.

PubMed: 21945315
DOI: 10.1016/j.febslet.2011.09.020

実験手法

X-RAY DIFFRACTION (2.2 Å)