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| | ==HADDOCK structure of the talin F3 domain in complex with talin 1655-1822== | | ==HADDOCK structure of the talin F3 domain in complex with talin 1655-1822== |
| - | <StructureSection load='2kgx' size='340' side='right'caption='[[2kgx]], [[NMR_Ensembles_of_Models | 2 NMR models]]' scene=''> | + | <StructureSection load='2kgx' size='340' side='right'caption='[[2kgx]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kgx]] is a 2 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=2KGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KGX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2kgx]] is a 2 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=2KGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KGX FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2kbb|2kbb]], [[2h7d|2h7d]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tln1, Tln ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Tln1, mKIAA1027 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kgx OCA], [https://pdbe.org/2kgx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kgx RCSB], [https://www.ebi.ac.uk/pdbsum/2kgx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kgx 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=2kgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kgx OCA], [https://pdbe.org/2kgx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kgx RCSB], [https://www.ebi.ac.uk/pdbsum/2kgx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kgx 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.
| + | [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: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Barsukov, I L]] | + | [[Category: Barsukov IL]] |
| - | [[Category: Bate, N]] | + | [[Category: Bate N]] |
| - | [[Category: Critchley, D R]] | + | [[Category: Critchley DR]] |
| - | [[Category: Gingras, A R]] | + | [[Category: Gingras AR]] |
| - | [[Category: Goult, B T]] | + | [[Category: Goult BT]] |
| - | [[Category: Cell adhesion]]
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| - | [[Category: Cell membrane]]
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| - | [[Category: Cell projection]]
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| - | [[Category: Cytoplasm]]
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| - | [[Category: Cytoskeleton]]
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| - | [[Category: F3]]
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| - | [[Category: Interdomain]]
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| - | [[Category: Membrane]]
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| - | [[Category: Phosphoprotein]]
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| - | [[Category: Talin]]
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| Structural highlights
Function
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
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Talin is a large flexible rod-shaped protein that activates the integrin family of cell adhesion molecules and couples them to cytoskeletal actin. It exists in both globular and extended conformations, and an intramolecular interaction between the N-terminal F3 FERM subdomain and the C-terminal part of the talin rod contributes to an autoinhibited form of the molecule. Here, we report the solution structure of the primary F3 binding domain within the C-terminal region of the talin rod and use intermolecular nuclear Overhauser effects to determine the structure of the complex. The rod domain (residues 1655-1822) is an amphipathic five-helix bundle; Tyr-377 of F3 docks into a hydrophobic pocket at one end of the bundle, whereas a basic loop in F3 (residues 316-326) interacts with a cluster of acidic residues in the middle of helix 4. Mutation of Glu-1770 abolishes binding. The rod domain competes with beta3-integrin tails for binding to F3, and the structure of the complex suggests that the rod is also likely to sterically inhibit binding of the FERM domain to the membrane.
The structure of an interdomain complex that regulates talin activity.,Goult BT, Bate N, Anthis NJ, Wegener KL, Gingras AR, Patel B, Barsukov IL, Campbell ID, Roberts GC, Critchley DR J Biol Chem. 2009 May 29;284(22):15097-106. Epub 2009 Mar 18. PMID:19297334[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Goult BT, Bate N, Anthis NJ, Wegener KL, Gingras AR, Patel B, Barsukov IL, Campbell ID, Roberts GC, Critchley DR. The structure of an interdomain complex that regulates talin activity. J Biol Chem. 2009 May 29;284(22):15097-106. Epub 2009 Mar 18. PMID:19297334 doi:10.1074/jbc.M900078200
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