3x23

Radixin complex

spinqualitylabelsall models 3x23, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3x23 is a 2 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.396Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RADI_MOUSE Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Radixin

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