Matrix metalloproteinase: Difference between revisions
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account for the entire binding effect between MT1-MMP and TIMP-1. Statistical analysis of the <scene name='MT1-MMP-TIMP-1_complex/Cv2/15'>key hydrogen bond</scene> stabilities in the TIMP-1 T98L mutant reveals that the hydrogen bonds network in mutant form is significantly more stable than that in WT-TIMP-1. Mutations that enhance hydrogen | account for the entire binding effect between MT1-MMP and TIMP-1. Statistical analysis of the <scene name='MT1-MMP-TIMP-1_complex/Cv2/15'>key hydrogen bond</scene> stabilities in the TIMP-1 T98L mutant reveals that the hydrogen bonds network in mutant form is significantly more stable than that in WT-TIMP-1. Mutations that enhance hydrogen | ||
bond stability contribute to the stability of the bound-like, less flexible, conformation of TIMP-1, which eventually results in increasing binding affinity for MT1-MMP. Thus, mutation affected the instrinsic dynamics of the inhibitor rather than its structure, thereby facilitating the interaction <ref name="Grossman">PMID:20545310</ref>. | bond stability contribute to the stability of the bound-like, less flexible, conformation of TIMP-1, which eventually results in increasing binding affinity for MT1-MMP. Thus, mutation affected the instrinsic dynamics of the inhibitor rather than its structure, thereby facilitating the interaction <ref name="Grossman">PMID:20545310</ref>. | ||
==3D structures of matrix metalloproteinase== | |||
[[Matrix metalloproteinase 3D structures]] | |||
</StructureSection> | </StructureSection> | ||
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*MMP13 collagenase 3 | *MMP13 collagenase 3 | ||
**[[1pex]] – hMMP hemopexin-like domain<br /> | **[[1pex]] – hMMP hemopexin-like domain<br /> | ||
**[[2yig]], [[3ljz]], [[3kec]], [[3kej]], [[3kek]], [[3kry]], [[3i7g]], [[3i7i]], [[3elm]], [[2pjt]], [[2ozr]], [[1xuc]], [[1xud]], [[1xur]], [[1you]], [[1ztq]], [[3o2x]], [[3zxh]], [[4a7b]], [[1fls]], [[1fm1]], [[456c]], [[830c]], [[3tvc]], [[4jp4]], [[4jpa]], [[3wv1]], [[3wv2]], [[3wv3]], [[4l19]], [[5b5o]], [[5b5p]], [[5bot]], [[5boy]], [[5bpa]] – hMMP catalytic domain + inhibitor<br /> | **[[2yig]], [[3ljz]], [[3kec]], [[3kej]], [[3kek]], [[3kry]], [[3i7g]], [[3i7i]], [[3elm]], [[2pjt]], [[2ozr]], [[1xuc]], [[1xud]], [[1xur]], [[1you]], [[1ztq]], [[3o2x]], [[3zxh]], [[4a7b]], [[1fls]], [[1fm1]], [[456c]], [[830c]], [[3tvc]], [[4jp4]], [[4jpa]], [[3wv1]], [[3wv2]], [[3wv3]], [[4l19]], [[5b5o]], [[5b5p]], [[5bot]], [[5boy]], [[5bpa]] – hMMP catalytic domain + inhibitor<br /> | ||
**[[2e2d]] - hMMP catalytic domain + TIMP-2<br /> | **[[2e2d]] - hMMP catalytic domain + TIMP-2<br /> | ||
**[[4fu4]], [[4fvl]], [[4g0d]] - hMMP catalytic domain (mutant) + pro-domain peptide<br /> | **[[4fu4]], [[4fvl]], [[4g0d]] - hMMP catalytic domain (mutant) + pro-domain peptide<br /> | ||
**[[6hv2]] - hMMP catalytic domain + peptide<br /> | |||
**[[1cxv]] - MMP catalytic domain - mouse<BR /> | |||
*MMP14 Membrane T1 | *MMP14 Membrane T1 | ||
**[[3ma2]] – hMMP residues 112-292 + TIMP-1 (mutant) <BR /> | **[[3ma2]] – hMMP residues 112-292 + TIMP-1 (mutant) <BR /> | ||
**[[1buv]], [[1bqq]] - hMMP + TIMP-2<BR /> | **[[1buv]], [[1bqq]] residues 112-292 hMMP + TIMP-2<BR /> | ||
**[[3c7x]] – hMMP hemopexin- | **[[5h0u]] - hMMP residues 112-292 + polyHis<br /> | ||
**[[3c7x]] – hMMP hemopexin domain residues 316-511<br /> | |||
**[[6cm1]], [[6clz]] – hMMP hemopexin domain + apolipoprotein<br /> | |||
**[[2mqs]] - hMMP + collagen<br /> | **[[2mqs]] - hMMP + collagen<br /> | ||
*MMP16 Membrane T3 | *MMP16 Membrane T3 | ||
