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| | ==Skelemin Immunoglobulin C2 like domain 4== | | ==Skelemin Immunoglobulin C2 like domain 4== |
| - | <StructureSection load='2jtd' size='340' side='right'caption='[[2jtd]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2jtd' size='340' side='right'caption='[[2jtd]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jtd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JTD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jtd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JTD FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Myom1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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'>[https://proteopedia.org/fgij/fg.htm?mol=2jtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jtd OCA], [https://pdbe.org/2jtd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jtd RCSB], [https://www.ebi.ac.uk/pdbsum/2jtd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jtd 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=2jtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jtd OCA], [https://pdbe.org/2jtd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jtd RCSB], [https://www.ebi.ac.uk/pdbsum/2jtd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jtd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MYOM1_MOUSE MYOM1_MOUSE]] May link the intermediate filament cytoskeleton to the M-disk of the myofibrils in striated muscle. May also contact myosin filaments. Also binds beta-integrins.
| + | [https://www.uniprot.org/uniprot/MYOM1_MOUSE MYOM1_MOUSE] May link the intermediate filament cytoskeleton to the M-disk of the myofibrils in striated muscle. May also contact myosin filaments. Also binds beta-integrins. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Deshmukh, L]] | + | [[Category: Deshmukh L]] |
| - | [[Category: Vinogradova, O]] | + | [[Category: Vinogradova O]] |
| - | [[Category: Cell adhesion]]
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| - | [[Category: Immune system]]
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| - | [[Category: Immunoglobulin domain]]
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| - | [[Category: Muscle protein]]
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| - | [[Category: Skelemin]]
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| - | [[Category: Thick filament]]
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| Structural highlights
Function
MYOM1_MOUSE May link the intermediate filament cytoskeleton to the M-disk of the myofibrils in striated muscle. May also contact myosin filaments. Also binds beta-integrins.
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
Skelemin is a large cytoskeletal protein critical for cell morphology. Previous studies have suggested that its two-tandem immunoglobulin C2-like repeats (SkIgC4 and SkIgC5) are involved in binding to integrin beta3 cytoplasmic tail (CT), providing a mechanism for skelemin to regulate integrin-mediated signaling and cell spreading. Using NMR spectroscopy, we have studied the molecular details of the skelemin IgC45 interaction with the cytoplasmic face of integrin alphaIIbbeta3. Here, we show that skelemin IgC45 domains form a complex not only with integrin beta3 CT but also, surprisingly, with the integrin alphaIIb CT. Chemical shift mapping experiments demonstrate that both membrane-proximal regions of alphaIIb and beta3 CTs are involved in binding to skelemin. NMR structural determinations, combined with homology modeling, revealed that SkIgC4 and SkIgC5 both exhibited a conserved Ig-fold and both repeats were required for effective binding to and attenuation of alphaIIbbeta3 cytoplasmic complex. These data provide the first molecular insight into how skelemin may interact with integrins and regulate integrin-mediated signaling and cell spreading.
Structural insight into the interaction between platelet integrin alphaIIbbeta3 and cytoskeletal protein skelemin.,Deshmukh L, Tyukhtenko S, Liu J, Fox JE, Qin J, Vinogradova O J Biol Chem. 2007 Nov 2;282(44):32349-56. Epub 2007 Sep 5. PMID:17804417[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Deshmukh L, Tyukhtenko S, Liu J, Fox JE, Qin J, Vinogradova O. Structural insight into the interaction between platelet integrin alphaIIbbeta3 and cytoskeletal protein skelemin. J Biol Chem. 2007 Nov 2;282(44):32349-56. Epub 2007 Sep 5. PMID:17804417 doi:10.1074/jbc.M704666200
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