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| | ==Solution structure of the 23th Filamin domain from human Filamin C== | | ==Solution structure of the 23th Filamin domain from human Filamin C== |
| - | <StructureSection load='2d7q' size='340' side='right' caption='[[2d7q]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2d7q' size='340' side='right'caption='[[2d7q]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2d7q]] is a 1 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=2D7Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2D7Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2d7q]] is a 1 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=2D7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D7Q FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FLNC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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> |
| - | <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=2d7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d7q OCA], [http://pdbe.org/2d7q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d7q RCSB], [http://www.ebi.ac.uk/pdbsum/2d7q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2d7q ProSAT], [http://www.topsan.org/Proteins/RSGI/2d7q TOPSAN]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2d7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d7q OCA], [https://pdbe.org/2d7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d7q RCSB], [https://www.ebi.ac.uk/pdbsum/2d7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d7q ProSAT], [https://www.topsan.org/Proteins/RSGI/2d7q TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/FLNC_HUMAN FLNC_HUMAN]] Defects in FLNC are the cause of myopathy myofibrillar type 5 (MFM5) [MIM:[http://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:[http://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> | + | [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 == | | == Function == |
| - | [[http://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. | + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Filamin|Filamin]] | + | *[[Filamin 3D structures|Filamin 3D structures]] |
| - | *[[Group:MUZIC:FilaminC|MUZIC:FilaminC]]
| + | |
| | *[[User:Georg Mlynek/workbench|User:Georg Mlynek/workbench]] | | *[[User:Georg Mlynek/workbench|User:Georg Mlynek/workbench]] |
| | == References == | | == References == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Inoue, M]] | + | [[Category: Large Structures]] |
| - | [[Category: Kigawa, T]] | + | [[Category: Inoue M]] |
| - | [[Category: Koshiba, S]] | + | [[Category: Kigawa T]] |
| - | [[Category: Structural genomic]] | + | [[Category: Koshiba S]] |
| - | [[Category: Tomizawa, T]] | + | [[Category: Tomizawa T]] |
| - | [[Category: Yokoyama, S]] | + | [[Category: Yokoyama S]] |
| - | [[Category: Beta-sandwich]]
| + | |
| - | [[Category: Filamin domain]]
| + | |
| - | [[Category: Immunoglobulin-like fold]]
| + | |
| - | [[Category: National project on protein structural and functional analyse]]
| + | |
| - | [[Category: Nppsfa]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| | [[Category: Z-disk]] | | [[Category: Z-disk]] |
| Structural highlights
Disease
FLNC_HUMAN Defects in FLNC are the cause of myopathy myofibrillar type 5 (MFM5) [MIM: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.[1] Defects in FLNC are the cause of myopathy distal type 4 (MPD4) [MIM: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.[2]
Function
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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Vorgerd M, van der Ven PF, Bruchertseifer V, Lowe T, Kley RA, Schroder R, Lochmuller H, Himmel M, Koehler K, Furst DO, Huebner A. A mutation in the dimerization domain of filamin c causes a novel type of autosomal dominant myofibrillar myopathy. Am J Hum Genet. 2005 Aug;77(2):297-304. Epub 2005 May 31. PMID:15929027 doi:10.1086/431959
- ↑ Duff RM, Tay V, Hackman P, Ravenscroft G, McLean C, Kennedy P, Steinbach A, Schoffler W, van der Ven PF, Furst DO, Song J, Djinovic-Carugo K, Penttila S, Raheem O, Reardon K, Malandrini A, Gambelli S, Villanova M, Nowak KJ, Williams DR, Landers JE, Brown RH Jr, Udd B, Laing NG. Mutations in the N-terminal actin-binding domain of filamin C cause a distal myopathy. Am J Hum Genet. 2011 Jun 10;88(6):729-40. Epub 2011 May 27. PMID:21620354 doi:10.1016/j.ajhg.2011.04.021
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