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4gwm

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<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=4gwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gwm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gwm RCSB], [http://www.ebi.ac.uk/pdbsum/4gwm 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=4gwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gwm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gwm RCSB], [http://www.ebi.ac.uk/pdbsum/4gwm PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/MEP1B_HUMAN MEP1B_HUMAN]] Membrane metallopeptidase that sheds many membrane-bound proteins. Known substrates include: FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10, tenascin-C. The presence of several pro-inflammatory cytokine among substrates implicate MEP1B in inflammation. It is also involved in tissue remodeling due to its capability to degrade extracellular matrix components.<ref>PMID:21693781</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 04:47, 25 December 2014

Crystal structure of human promeprin beta

4gwm, resolution 1.85Å

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