1u89: Difference between revisions
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==Solution structure of VBS2 fragment of talin== | ==Solution structure of VBS2 fragment of talin== | ||
<StructureSection load='1u89' size='340' side='right'caption='[[1u89 | <StructureSection load='1u89' size='340' side='right'caption='[[1u89]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1u89]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1u89]] 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=1U89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U89 FirstGlance]. <br> | ||
</td></tr><tr id=' | </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=1u89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u89 OCA], [https://pdbe.org/1u89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u89 RCSB], [https://www.ebi.ac.uk/pdbsum/1u89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u89 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=1u89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u89 OCA], [https://pdbe.org/1u89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u89 RCSB], [https://www.ebi.ac.uk/pdbsum/1u89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u89 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/TLN1_MOUSE TLN1_MOUSE] Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts. | |||
== 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== | ||
*[[Talin|Talin]] | *[[Talin 3D structures|Talin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Barsukov | [[Category: Barsukov IL]] | ||
[[Category: Critchley | [[Category: Critchley DR]] | ||
[[Category: Emsley | [[Category: Emsley J]] | ||
[[Category: Fillingham | [[Category: Fillingham I]] | ||
[[Category: Gingras | [[Category: Gingras AR]] | ||
[[Category: Papagrigoriou | [[Category: Papagrigoriou E]] | ||
[[Category: Patel | [[Category: Patel B]] | ||
[[Category: Roberts | [[Category: Roberts GCK]] | ||
Latest revision as of 16:14, 9 May 2024
Solution structure of VBS2 fragment of talinSolution structure of VBS2 fragment of talin
Structural highlights
FunctionTLN1_MOUSE Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts. 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 PubMedThe cytoskeletal protein talin plays a key role in activating integrins and in coupling them to the actin cytoskeleton. Its N-terminal globular head, which binds beta integrins, is linked to an extended rod having a C-terminal actin binding site and several vinculin binding sites (VBSs). The NMR structure of residues 755-889 of the rod (containing a VBS) is shown to be an amphipathic four-helix bundle with a left-handed topology. A talin peptide corresponding to the VBS binds the vinculin head; the X-ray crystallographic structure of this complex shows that the residues which interact with vinculin are buried in the hydrophobic core of the talin fragment. NMR shows that the interaction involves a major structural change in the talin fragment, including unfolding of one of its helices, making the VBS accessible to vinculin. Interestingly, the talin 755-889 fragment binds more than one vinculin head molecule, suggesting that the talin rod may contain additional as yet unrecognized VBSs. A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head.,Fillingham I, Gingras AR, Papagrigoriou E, Patel B, Emsley J, Critchley DR, Roberts GC, Barsukov IL Structure. 2005 Jan;13(1):65-74. PMID:15642262[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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