Literature summary for 3.4.24.22 extracted from

Batra, J.; Soares, A.; Mehner, C.; Radisky, E.
Matrix metalloproteinase-10/TIMP-2 structure and analyses define conserved core interactions and diverse exosite interactions in MMP/TIMP complexes (2013), PLoS ONE, 8, e75836.

Search for more literature for 3.4.24.22

Cloned(Commentary)

Cloned (Comment)	Organism
expression of the enzyme catalytic domain in Escherichia coli strain BL21 (DE3)	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified active human MMP-10 catalytic domain in complex with inhibitor protein TIMP-2, hanging drop vapor diffusion method, mixing of proteins in a 1:1.1 (mol/mol) ratio, 4.5-5.5 mg/ml protein in 20 mM Tris, pH 8.5 and 150 mM NaCl, are mixed with reservoir solution containing 0.1 M HEPES, pH 7.5, and 25% w/v PEG 2000 monomethyl ether, 1-2 weeks, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement, comparison and analysis of the crystal structure of the human MMP-10/TIMP-1 complex, PDB ID 3V96	Homo sapiens

Crystallization (Comment)

Organism

purified active human MMP-10 catalytic domain in complex with inhibitor protein TIMP-2, hanging drop vapor diffusion method, mixing of proteins in a 1:1.1 (mol/mol) ratio, 4.5-5.5 mg/ml protein in 20 mM Tris, pH 8.5 and 150 mM NaCl, are mixed with reservoir solution containing 0.1 M HEPES, pH 7.5, and 25% w/v PEG 2000 monomethyl ether, 1-2 weeks, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement, comparison and analysis of the crystal structure of the human MMP-10/TIMP-1 complex, PDB ID 3V96

Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	the endogenous tissue inhibitors of metalloproteinases (TIMPs) regulate proteolytic activity by binding tightly to the MMP active site. While each of the four TIMPs can inhibit most MMPs, binding data reveal tremendous heterogeneity in affinities of different TIMP/MMP pairs. Identification of a group of highly conserved contacts at the heart of MMP/TIMP complexes that define the conserved mechanism of inhibition, as well as a second category of diverse adventitious contacts at the periphery of the interfaces	Homo sapiens
tissue inhibitor of metalloproteinases 2	TIMP-2, conserved mechanism of inhibition, interactions and conformation analysis, and structural changes induced by complex formation with the enzyme's catalytic domain, detailed overview	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P16035	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme MMP-10 catalytic domain from Escherichia coli strain BL21 (DE3), by anion exchange chromatography and gel filtration	Homo sapiens

Synonyms

Synonyms	Comment	Organism
Matrix metalloproteinase-10	-	Homo sapiens
MMP-10	-	Homo sapiens

General Information

General Information	Comment	Organism
metabolism	matrix metalloproteinases (MMPs) play central roles in vertebrate tissue development, remodeling, and repair. The endogenous tissue inhibitors of metalloproteinases (TIMPs) regulate proteolytic activity by binding tightly to the MMP active site. While each of the four TIMPs can inhibit most MMPs, binding data reveal tremendous heterogeneity in affinities of different TIMP/MMP pairs	Homo sapiens