3c7x: Difference between revisions

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==Hemopexin-like domain of matrix metalloproteinase 14==
==Hemopexin-like domain of matrix metalloproteinase 14==
<StructureSection load='3c7x' size='340' side='right' caption='[[3c7x]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3c7x' size='340' side='right' caption='[[3c7x]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane-type_matrix_metalloproteinase-1 Membrane-type matrix metalloproteinase-1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.80 3.4.24.80] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane-type_matrix_metalloproteinase-1 Membrane-type matrix metalloproteinase-1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.80 3.4.24.80] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c7x OCA], [http://pdbe.org/3c7x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c7x RCSB], [http://www.ebi.ac.uk/pdbsum/3c7x PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c7x OCA], [http://pdbe.org/3c7x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c7x RCSB], [http://www.ebi.ac.uk/pdbsum/3c7x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3c7x ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c7/3c7x_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c7/3c7x_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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==See Also==
==See Also==
*[[Matrix metalloproteinase|Matrix metalloproteinase]]
*[[Matrix metalloproteinase|Matrix metalloproteinase]]
*[[Molecular Playground/MMP14|Molecular Playground/MMP14]]
== References ==
== References ==
<references/>
<references/>

Revision as of 09:05, 20 June 2018

Hemopexin-like domain of matrix metalloproteinase 14Hemopexin-like domain of matrix metalloproteinase 14

Structural highlights

3c7x is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Activity:Membrane-type matrix metalloproteinase-1, with EC number 3.4.24.80
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MMP14_HUMAN] Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Homodimerization is an essential step for membrane type 1 matrix metalloproteinase (MT1-MMP) to activate proMMP-2 and to degrade collagen on the cell surface. To uncover the molecular basis of the hemopexin (Hpx) domain-driven dimerization of MT1-MMP, a crystal structure of the Hpx domain was solved at 1.7 A resolution. Two interactions were identified as potential biological dimer interfaces in the crystal structure, and mutagenesis studies revealed that the biological dimer possesses a symmetrical interaction where blades II and III of molecule A interact with blades III and II of molecule B. The mutations of amino acids involved in the interaction weakened the dimer interaction of Hpx domains in solution, and incorporation of these mutations into the full-length enzyme significantly inhibited dimer-dependent functions on the cell surface, including proMMP-2 activation, collagen degradation, and invasion into the three-dimensional collagen matrix, whereas dimer-independent functions, including gelatin film degradation and two-dimensional cell migration, were not affected. These results shed light on the structural basis of MT1-MMP dimerization that is crucial to promote cellular invasion.

The dimer interface of the membrane type 1 matrix metalloproteinase hemopexin domain: crystal structure and biological functions.,Tochowicz A, Goettig P, Evans R, Visse R, Shitomi Y, Palmisano R, Ito N, Richter K, Maskos K, Franke D, Svergun D, Nagase H, Bode W, Itoh Y J Biol Chem. 2011 Mar 4;286(9):7587-600. Epub 2010 Dec 30. PMID:21193411[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Golubkov VS, Chekanov AV, Cieplak P, Aleshin AE, Chernov AV, Zhu W, Radichev IA, Zhang D, Dong PD, Strongin AY. The Wnt/planar cell polarity protein-tyrosine kinase-7 (PTK7) is a highly efficient proteolytic target of membrane type-1 matrix metalloproteinase: implications in cancer and embryogenesis. J Biol Chem. 2010 Nov 12;285(46):35740-9. doi: 10.1074/jbc.M110.165159. Epub 2010, Sep 13. PMID:20837484 doi:http://dx.doi.org/10.1074/jbc.M110.165159
  2. Gu G, Zhao D, Yin Z, Liu P. BST-2 binding with cellular MT1-MMP blocks cell growth and migration via decreasing MMP2 activity. J Cell Biochem. 2012 Mar;113(3):1013-21. doi: 10.1002/jcb.23433. PMID:22065321 doi:10.1002/jcb.23433
  3. Tochowicz A, Goettig P, Evans R, Visse R, Shitomi Y, Palmisano R, Ito N, Richter K, Maskos K, Franke D, Svergun D, Nagase H, Bode W, Itoh Y. The dimer interface of the membrane type 1 matrix metalloproteinase hemopexin domain: crystal structure and biological functions. J Biol Chem. 2011 Mar 4;286(9):7587-600. Epub 2010 Dec 30. PMID:21193411 doi:10.1074/jbc.M110.178434

3c7x, resolution 1.70Å

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OCA