3v8o: Difference between revisions

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<StructureSection load='3v8o' size='340' side='right'caption='[[3v8o]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='3v8o' size='340' side='right'caption='[[3v8o]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3v8o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V8O FirstGlance]. <br>
<table><tr><td colspan='2'>[[3v8o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V8O FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABPL, FLN2, FLNC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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=3v8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v8o OCA], [https://pdbe.org/3v8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v8o RCSB], [https://www.ebi.ac.uk/pdbsum/3v8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v8o ProSAT]</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=3v8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v8o OCA], [https://pdbe.org/3v8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v8o RCSB], [https://www.ebi.ac.uk/pdbsum/3v8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v8o ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[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>
[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 ==
[[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.  
[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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Immunoglobulin-like (Ig) domains are a widely expanded superfamily that acts as interaction motifs or as structural spacers in multi-domain proteins. Vertebrate filamins (FLNs), which are multifunctional actin binding proteins, consists of 24 Ig domains. We have recently discovered that in the C-terminal Rod 2 region of FLN, Ig domains interact with each other forming functional domain pairs, where the interaction with signaling and transmembrane proteins is mechanically regulated by weak actomyosin contraction forces. Here, we investigated if there are similar inter-domain interactions around domain 4 in the N-terminal Rod 1 region of FLN. Protein crystal structures revealed a new type of domain organization between domains 3, 4 and 5. In this module, domains 4 and 5 interact rather tightly whereas domain 3 has a partially flexible interface with domain 4. NMR peptide titration experiments showed that within the three domain module, domain 4 is capable for interaction with a peptide derived from platelet glycoprotein Ib. Crystal structure of FLN domains 4 and 5 in complex with the peptide revealed a typical beta sheet augmentation interaction observed for many FLN ligands. Domain 5 was found to stabilize domain 4, and this could provide a mechanism for the regulation of domain 4 interactions.
 
A Novel Structural Unit in the N-Terminal Region of Filamins.,Sethi R, Seppala J, Tossavainen H, Ylilauri M, Ruskamo S, Pentikainen OT, Pentikainen U, Permi P, Ylanne J J Biol Chem. 2014 Jan 27. PMID:24469451<ref>PMID:24469451</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3v8o" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sethi, R]]
[[Category: Sethi R]]
[[Category: Ylanne, J]]
[[Category: Ylanne J]]
[[Category: Immunoglobulin like fold]]
[[Category: Z-disk]]
[[Category: Structural protein]]
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