2k9u: Difference between revisions

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 ==Solution NMR structure of the Filamin-migfilin complex==
-<StructureSection load='2k9u' size='340' side='right' caption='[[2k9u]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2k9u' size='340' side='right'caption='[[2k9u]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2k9u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K9U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2k9u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K9U FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k9u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k9u RCSB], [http://www.ebi.ac.uk/pdbsum/2k9u PDBsum]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<table>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2k9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k9u OCA], [https://pdbe.org/2k9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k9u RCSB], [https://www.ebi.ac.uk/pdbsum/2k9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k9u ProSAT]</span></td></tr>
-<div style="background-color:#fffaf0;">
+</table>
-== Publication Abstract from PubMed ==
+== Disease ==
-The linkage of heterodimeric (alpha/beta) integrin receptors with their extracellular matrix ligands and intracellular actin cytoskeleton is a fundamental step for controlling cell adhesion and migration. Binding of the actin-linking protein, talin, to integrin beta cytoplasmic tails (CTs) induces high affinity ligand binding (integrin activation), whereas binding of another actin-linking protein, filamin, to the integrin beta CTs negatively regulates this process by blocking the talin-integrin interaction. Here we show structurally that migfilin, a novel cytoskeletal adaptor highly enriched in the integrin adhesion sites, strongly interacts with the same region in filamin where integrin beta CTs bind. We further demonstrate that the migfilin interaction dissociates filamin from integrin and promotes the talin/integrin binding and integrin activation. Migfilin thus acts as a molecular switch to disconnect filamin from integrin for regulating integrin activation and dynamics of extracellular matrix-actin linkage.
+[https://www.uniprot.org/uniprot/FLNC_HUMAN FLNC_HUMAN] Defects in FLNC are the cause of myopathy myofibrillar type 5 (MFM5) [MIM:[https://omim.org/entry/609524 609524]. A neuromuscular disorder, usually with an adult onset, characterized by focal myofibrillar destruction and pathological cytoplasmic protein aggregations, and clinical features of a limb-girdle myopathy.<ref>PMID:15929027</ref>   Defects in FLNC are the cause of myopathy distal type 4 (MPD4) [MIM:[https://omim.org/entry/614065 614065]. MPD4 is a slowly progressive muscular disorder characterized by distal muscle weakness and atrophy affecting the upper and lower limbs. Onset occurs around the third to fourth decades of life, and patients remain ambulatory even after long disease duration. Muscle biopsy shows non-specific changes with no evidence of rods, necrosis, or inflammation.<ref>PMID:21620354</ref>
+== Function ==
-Migfilin, a molecular switch in regulation of integrin activation.,Ithychanda SS, Das M, Ma YQ, Ding K, Wang X, Gupta S, Wu C, Plow EF, Qin J J Biol Chem. 2009 Feb 13;284(7):4713-22. doi: 10.1074/jbc.M807719200. Epub 2008, Dec 13. PMID:19074766<ref>PMID:19074766</ref>
+[https://www.uniprot.org/uniprot/FLNC_HUMAN FLNC_HUMAN] Muscle-specific filamin, which plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. May be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. Critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers.
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 ==See Also==
-*[[Filamin|Filamin]]
+*[[Filamin 3D structures|Filamin 3D structures]]
 *[[User:Georg Mlynek/workbench|User:Georg Mlynek/workbench]]
 == References ==
@@ Line 21: / Line 19: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Ithychanda, S N.]]
+[[Category: Large Structures]]
-[[Category: Qin, J.]]
+[[Category: Ithychanda SN]]
-[[Category: Cell adhesion]]
+[[Category: Qin J]]
-[[Category: Cell junction]]
-[[Category: Cell shape]]
-[[Category: Cytoskeletal complex]]
-[[Category: Cytoskeleton]]
-[[Category: Lim domain]]
-[[Category: Metal-binding]]
-[[Category: Structural protein]]