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Structure paper

TitleDirected evolution of the metalloproteinase inhibitor TIMP-1 reveals that its N- and C-terminal domains cooperate in matrix metalloproteinase recognition.
Journal, issue, pagesJ. Biol. Chem., Vol. 294, Page 9476-9488, Year 2019
Publish dateAug 28, 2018 (structure data deposition date)
AuthorsRaeeszadeh-Sarmazdeh, M. / Greene, K.A. / Sankaran, B. / Downey, G.P. / Radisky, D.C. / Radisky, E.S.
External linksJ. Biol. Chem. / PubMed:31040180
MethodsX-ray diffraction
Resolution2.37 - 2.67 Å
Structure data

PDB-6mav:
Complex of tissue inhibitor of metalloproteinase-1 (TIMP-1) mutant L34G with matrix metalloproteinase-3 catalytic domain (MMP-3cd)
Method: X-RAY DIFFRACTION / Resolution: 2.37 Å

PDB-6n9d:
Complex of tissue inhibitor of metalloproteinases-1 (TIMP-1) mutant (L34G/L133P/L151C/G154A) with matrix metalloproteinase-3 catalytic domain (MMP-3cd)
Method: X-RAY DIFFRACTION / Resolution: 2.67 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE/HYDROLASE inhibitor / Protease inhibitor / Matrix metalloproteinase-3 (MMP-3) / Tissue inhibitor of metalloproteinase-1 (TIMP-1) / HYDROLASE-HYDROLASE inhibitor complex / tissue inhibitor of metalloproteinases / matrix metalloproteinase / HYDROLASE

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