3SHI

Crystal structure of human MMP1 catalytic domain at 2.2 A resolution

Summary for 3SHI

• Entry DOI: 10.2210/pdb3shi/pdb
• Related: 1CGE 1HFC 966C
• Descriptor: Interstitial collagenase, ZINC ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: matrix metalloproteinase, paramagnetic restraints, paramagnetic tag, lanthanides, protein refinement, residual dipolar couplings, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix : P03956
• Total number of polymer chains: 3
• Total formula weight: 53127.11

Authors

Bertini, I.,Calderone, V.,Cerofolini, L.,Fragai, M.,Geraldes, C.F.G.C.,Hermann, P.,Luchinat, C.,Parigi, G.,Teixeira, J. (deposition date: 2011-06-16, release date: 2011-09-21, Last modification date: 2023-09-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)