2nqc

From Proteopedia

(Difference between revisions)

Revision as of 13:20, 19 January 2015

Crystal structure of ig-like domain 23 from human filamin C

Structural highlights

2nqc is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Resources:	FirstGlance, OCA, RCSB, PDBsum

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.

Publication Abstract from PubMed

Filamin C is a dimeric, actin-binding protein involved in organization of cortical cytoskeleton and of the sarcomere. We performed crystallographic, small-angle X-ray scattering and analytical ultracentrifugation experiments on the constructs containing carboxy-terminal domains of the protein (domains 23-24 and 19-21). The crystal structure of domain 23 of filamin C showed that the protein adopts the expected immunoglobulin (Ig)-like fold. Small-angle X-ray scattering experiments performed on filamin C tandem Ig-like domains 23 and 24 reveal a dimer that is formed by domain 24 and that domain 23 has little interactions with itself or with domain 24, while the analytical ultracentrifugation experiments showed that the filamin C domains 19-21 form elongated monomers in diluted solutions.

Crystal structure of human filamin C domain 23 and small angle scattering model for filamin C 23-24 dimer.,Sjekloca L, Pudas R, Sjoblom B, Konarev P, Carugo O, Rybin V, Kiema TR, Svergun D, Ylanne J, Djinovic Carugo K J Mol Biol. 2007 May 11;368(4):1011-23. Epub 2007 Feb 20. PMID:17379241^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ Sjekloca L, Pudas R, Sjoblom B, Konarev P, Carugo O, Rybin V, Kiema TR, Svergun D, Ylanne J, Djinovic Carugo K. Crystal structure of human filamin C domain 23 and small angle scattering model for filamin C 23-24 dimer. J Mol Biol. 2007 May 11;368(4):1011-23. Epub 2007 Feb 20. PMID:17379241 doi:10.1016/j.jmb.2007.02.018

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2nqc"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2nqc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NQC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NQC FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></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=2nqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nqc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2nqc RCSB], [http://www.ebi.ac.uk/pdbsum/2nqc 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=2nqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nqc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2nqc RCSB], [http://www.ebi.ac.uk/pdbsum/2nqc PDBsum]</span></td></tr>
-<table>
+</table>
 == 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>
@@ Line 38: / Line 38: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Carugo, O.]]
+[[Category: Carugo, O]]
-[[Category: Djinovic-Carugo, K.]]
+[[Category: Djinovic-Carugo, K]]
-[[Category: Kiema, T R.]]
+[[Category: Kiema, T R]]
-[[Category: Konarev, P.]]
+[[Category: Konarev, P]]
-[[Category: Pudas, R.]]
+[[Category: Pudas, R]]
-[[Category: Rybin, V.]]
+[[Category: Rybin, V]]
-[[Category: Sjekloca, L.]]
+[[Category: Sjekloca, L]]
-[[Category: Sjoeblom, B.]]
+[[Category: Sjoeblom, B]]
-[[Category: Svergun, D.]]
+[[Category: Svergun, D]]
-[[Category: Ylanne, J.]]
+[[Category: Ylanne, J]]
 [[Category: Filamin]]
 [[Category: Immune system]]
 [[Category: Immunoglobulin]]
 [[Category: Metal binding]]

2nqc

From Proteopedia

Revision as of 13:20, 19 January 2015

Crystal structure of ig-like domain 23 from human filamin C

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox