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2cum

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Current revision (11:31, 22 May 2024) (edit) (undo)
 
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==The solution structure of the 33rd fibronectin type III domain of human Tenascin-X==
==The solution structure of the 33rd fibronectin type III domain of human Tenascin-X==
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<StructureSection load='2cum' size='340' side='right'caption='[[2cum]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2cum' size='340' side='right'caption='[[2cum]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2cum]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CUM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2cum]] 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=2CUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CUM FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TNXB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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</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=2cum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cum OCA], [https://pdbe.org/2cum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cum RCSB], [https://www.ebi.ac.uk/pdbsum/2cum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cum ProSAT], [https://www.topsan.org/Proteins/RSGI/2cum 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=2cum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cum OCA], [https://pdbe.org/2cum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cum RCSB], [https://www.ebi.ac.uk/pdbsum/2cum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cum ProSAT], [https://www.topsan.org/Proteins/RSGI/2cum TOPSAN]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/TENX_HUMAN TENX_HUMAN]] Defects in TNXB are the cause of tenascin-X deficiency (TNXD) [MIM:[https://omim.org/entry/606408 606408]]. TNXD leads to an Ehlers-Danlos-like syndrome characterized by hyperextensible skin, hypermobile joints, and tissue fragility. Tenascin-X-deficient patients, however, lack atrophic scars, a major diagnostic criteria for classic Ehlers-Danlos. Delayed wound healing, which is also common in classic EDS, is only present in a subset of patients.
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[https://www.uniprot.org/uniprot/TENX_HUMAN TENX_HUMAN] Defects in TNXB are the cause of tenascin-X deficiency (TNXD) [MIM:[https://omim.org/entry/606408 606408]. TNXD leads to an Ehlers-Danlos-like syndrome characterized by hyperextensible skin, hypermobile joints, and tissue fragility. Tenascin-X-deficient patients, however, lack atrophic scars, a major diagnostic criteria for classic Ehlers-Danlos. Delayed wound healing, which is also common in classic EDS, is only present in a subset of patients.
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/TENX_HUMAN TENX_HUMAN]] Appears to mediate interactions between cells and the extracellular matrix. Substrate-adhesion molecule that appears to inhibit cell migration. Accelerates collagen fibril formation. May play a role in supporting the growth of epithelial tumors.<ref>PMID:17033827</ref>
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[https://www.uniprot.org/uniprot/TENX_HUMAN TENX_HUMAN] Appears to mediate interactions between cells and the extracellular matrix. Substrate-adhesion molecule that appears to inhibit cell migration. Accelerates collagen fibril formation. May play a role in supporting the growth of epithelial tumors.<ref>PMID:17033827</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Inoue, M]]
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[[Category: Inoue M]]
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[[Category: Kigawa, T]]
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[[Category: Kigawa T]]
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[[Category: Koshiba, S]]
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[[Category: Koshiba S]]
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[[Category: Structural genomic]]
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[[Category: Tochio N]]
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[[Category: Tochio, N]]
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[[Category: Yokoyama S]]
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[[Category: Yokoyama, S]]
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[[Category: Cell adhesion]]
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[[Category: Fibronectin type iii domain]]
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[[Category: Hexabrachion-like]]
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[[Category: National project on protein structural and functional analyse]]
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[[Category: Nppsfa]]
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[[Category: Rsgi]]
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Current revision

The solution structure of the 33rd fibronectin type III domain of human Tenascin-X

PDB ID 2cum

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