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Crystal structure of human MMP1 catalytic domain at 2.2 A resolutionCrystal structure of human MMP1 catalytic domain at 2.2 A resolution
Structural highlights
Function[MMP1_HUMAN] Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.[1] Publication Abstract from PubMedPseudocontact 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. The catalytic domain of MMP-1 studied through tagged lanthanides.,Bertini I, Calderone V, Cerofolini L, Fragai M, Geraldes CF, Hermann P, Luchinat C, Parigi G, Teixeira JM FEBS Lett. 2011 Sep 19. PMID:21945315[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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