MT1-MMP-TIMP-1 complex: Difference between revisions

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Alexander Berchansky, Michal Harel

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 <StructureSection load='M1.pdb' size='500' side='right' scene='MT1-MMP-TIMP-1_complex/Cv2/1' caption=''>
-The human matrix metalloproteinases (MMPs) family comprises a large group of structurally homologous zinc-dependent endopeptidases (e.g. <scene name='MT1-MMP-TIMP-1_complex/Cv2/2'>Membrane type-1 matrix metalloproteinase (MT1-MMP)</scene> and <scene name='MT1-MMP-TIMP-1_complex/Cv/9'>Membrane type-3 matrix metalloproteinase (MT3-MMP)</scene> that perform a wide variety of biological roles. The MMPs are in general inhibited unselectively by all 4 known tissue inhibitors of metalloproteinases (TIMP) TIMPs (TIMP 1-4). Currently, four tissue inhibitor of metalloproteinases (TIMP) variants that are 40-50% identical in sequence have been identified, namely TIMP-1-4. In general, the MMPs are  inhibited unselectively by all 4 known TIMPs (TIMP 1-4). <scene name='MT1-MMP-TIMP-1_complex/Cv2/2'>Membrane type-1 matrix metalloproteinase (MT1-MMP)</scene> <font color='violet'><b>(violet)</b></font> forms complex with <scene name='MT1-MMP-TIMP-1_complex/Cv2/4'>wild-type tissue inhibitor of metalloproteinase-1 (TIMP-1)</scene> ([[2j0t]], <font color='lime'><b>colored lime</b></font>).
+The human matrix metalloproteinases (MMPs) family comprises a large group of structurally homologous zinc-dependent endopeptidases (''e.g.'' <scene name='MT1-MMP-TIMP-1_complex/Cv2/2'>Membrane type-1 matrix metalloproteinase (MT1-MMP)</scene> <font color='violet'><b>(violet)</b></font> and <scene name='MT1-MMP-TIMP-1_complex/Cv/9'>Membrane type-3 matrix metalloproteinase (MT3-MMP)</scene> <font color='magenta'><b>(magenta)</b></font>, <scene name='MT1-MMP-TIMP-1_complex/Cv2/6'>click to see morph</scene>) that perform a wide variety of biological roles. The MMPs are in general inhibited unselectively by all 4 known tissue inhibitors of metalloproteinases (TIMP) TIMPs (TIMP 1-4). Currently, four tissue inhibitor of metalloproteinases (TIMP) variants that are 40-50% identical in sequence have been identified, namely TIMP-1-4. In general, the MMPs are  inhibited unselectively by all 4 known TIMPs (TIMP 1-4). <scene name='MT1-MMP-TIMP-1_complex/Cv2/2'>Membrane type-1 matrix metalloproteinase (MT1-MMP)</scene> <font color='violet'><b>(violet)</b></font> forms complex with <scene name='MT1-MMP-TIMP-1_complex/Cv2/4'>wild-type tissue inhibitor of metalloproteinase-1 (TIMP-1)</scene> ([[2j0t]], <font color='lime'><b>colored lime</b></font>).
-<scene name='MT1-MMP-TIMP-1_complex/Cv/9'>Membrane type-3 matrix metalloproteinase (MT3-MMP)</scene> <font color='magenta'><b>(magenta)</b></font> forms complex with <scene name='MT1-MMP-TIMP-1_complex/Cv/12'>wild-type TIMP-1</scene> ([[1uea]], <font color='orange'><b>colored orange</b></font>). <scene name='MT1-MMP-TIMP-1_complex/Cv/13'>The WT-TIMP-1 binding interface</scene> <font color='cyan'><b>(cyan)</b></font> is mainly composed of the N-terminal segment that approaches the active site, the AB loop (Thr33-Tyr35), the CD loop (Ala65-Cys70), and the EF loop (Thr97-Ser100). The pivotal residue, threonine 98 (Thr98), is shown as <font color='red'><b>red sticks</b></font>. In general, <scene name='MT1-MMP-TIMP-1_complex/Cv1/2'>five main chain hydrogen bonds</scene> (Cys1-Ser68, Val69-Met66, Gly71-Met66, Cys70-Glu67, and Cys70-Thr98) are intimately involved in the conformational stability of TIMP binding interface when bound to MMP.
+<scene name='MT1-MMP-TIMP-1_complex/Cv/9'>Membrane type-3 matrix metalloproteinase (MT3-MMP)</scene>  forms complex with <scene name='MT1-MMP-TIMP-1_complex/Cv/12'>wild-type TIMP-1</scene> ([[1uea]], <font color='orange'><b>colored orange</b></font>). <scene name='MT1-MMP-TIMP-1_complex/Cv/13'>The WT-TIMP-1 binding interface</scene> <font color='cyan'><b>(cyan)</b></font> is mainly composed of the N-terminal segment that approaches the active site, the AB loop (Thr33-Tyr35), the CD loop (Ala65-Cys70), and the EF loop (Thr97-Ser100). The pivotal residue, threonine 98 (Thr98), is shown as <font color='red'><b>red sticks</b></font>. In general, <scene name='MT1-MMP-TIMP-1_complex/Cv1/2'>five main chain hydrogen bonds</scene> (Cys1-Ser68, Val69-Met66, Gly71-Met66, Cys70-Glu67, and Cys70-Thr98) are intimately involved in the conformational stability of TIMP binding interface when bound to MMP.
 </StructureSection>
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