Tyrosine 36 Plays a Critical Role in the Interaction of the AB Loop of Tissue Inhibitor of Metalloproteinases-2 with Matrix Metalloproteinase-14

The tissue inhibitor of metalloproteinases-2 (TIMP-2) is potentially an important inhibitor of all known matrix metalloproteinases (MMPs). However, it has been shown to undergo specific interactions with both MMP-2 (gelatinase A) and MMP-14 (MT1-MMP), and it has been proposed that these three protei...

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Veröffentlicht in:	The Journal of biological chemistry 2001-08, Vol.276 (35), p.32966-32970
Hauptverfasser:	Williamson, Richard A., Hutton, Mike, Vogt, Gavin, Rapti, Magdalene, Knäuper, Vera, Carr, Mark D., Murphy, Gillian
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acid Substitution Binding Sites Crystallography, X-Ray Humans Kinetics matrix metalloproteinase 14 Matrix Metalloproteinases, Membrane-Associated Metalloendopeptidases - chemistry Metalloendopeptidases - metabolism Models, Molecular Molecular Sequence Data MT1-MMP protein Mutagenesis, Site-Directed Protein Conformation Protein Denaturation Protein Structure, Secondary Recombinant Proteins - chemistry Recombinant Proteins - metabolism Sequence Alignment Sequence Deletion Sequence Homology, Amino Acid TIMP-2 protein tissue inhibitor of matrix metalloproteinases-2 Tissue Inhibitor of Metalloproteinase-2 - chemistry Tissue Inhibitor of Metalloproteinase-2 - metabolism Tyrosine
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