3x23
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Radixin complex== |
| + | <StructureSection load='3x23' size='340' side='right' caption='[[3x23]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3x23]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3X23 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3X23 FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gc7|1gc7]], [[1j19|1j19]], [[2yvc|2yvc]], [[2ems|2ems]], [[2emt|2emt]], [[2d2q|2d2q]], [[1gc6|1gc6]], [[2d10|2d10]], [[2d11|2d11]], [[1isn|1isn]], [[2zpy|2zpy]]</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=3x23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x23 OCA], [http://pdbe.org/3x23 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3x23 RCSB], [http://www.ebi.ac.uk/pdbsum/3x23 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/RADI_MOUSE RADI_MOUSE]] Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane. [[http://www.uniprot.org/uniprot/MMP14_HUMAN 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.<ref>PMID:20837484</ref> <ref>PMID:22065321</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Membrane type 1-matrix metalloproteinase (MT1-MMP) is a key enzyme involved in tumor cell invasion by shedding their cell-surface receptor CD44 anchored with F-actin through ezrin/radixin/moesin (ERM) proteins. We found the cytoplasmic tail of MT1-MMP directly binds the FERM domain of radixin, suggesting F-actin-based recruitment of MT1-MMP to CD44 for invasion. Our crystal structure shows that the central region of the MT1-MMP cytoplasmic tail binds subdomain A of the FERM domain, and makes an antiparallel beta-beta interaction with beta2A-strand. This binding mode is distinct from the previously determined binding mode of CD44 to subdomain C. We showed that radixin simultaneously binds both MT1-MMP and CD44, indicating ERM protein-mediated colocalization of MT1-MMP and its substrate CD44 and anchoring to F-actin. Our study implies that ERM proteins contribute toward accelerated CD44 shedding by MT1-MMP through ERM protein-mediated interactions between their cytoplasmic tails. | ||
| - | + | MT1-MMP recognition by ERM proteins and its implication in CD44 shedding.,Terawaki S, Kitano K, Aoyama M, Mori T, Hakoshima T Genes Cells. 2015 Oct;20(10):847-59. doi: 10.1111/gtc.12276. Epub 2015 Aug 20. PMID:26289026<ref>PMID:26289026</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3x23" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Aoyama, M]] | [[Category: Aoyama, M]] | ||
| + | [[Category: Hakoshima, T]] | ||
| + | [[Category: Kitano, K]] | ||
[[Category: Mori, T]] | [[Category: Mori, T]] | ||
[[Category: Terawaki, S]] | [[Category: Terawaki, S]] | ||
| - | [[Category: | + | [[Category: Adhesion receptor]] |
| - | [[Category: | + | [[Category: Cell adhesion]] |
| + | [[Category: Cell invasion]] | ||
| + | [[Category: Ferm domain]] | ||
Revision as of 05:27, 22 October 2015
Radixin complex
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