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| - | ==STRUCTURE OF THE TALIN ROD RESIDUES 1359-1659== | + | ==Crystal Structure of the R7R8 domains of Talin== |
| - | <StructureSection load='2x0c' size='340' side='right' caption='[[2x0c]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='2x0c' size='340' side='right'caption='[[2x0c]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2x0c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X0C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X0C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2x0c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X0C FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1y19|1y19]], [[1u89|1u89]], [[1t01|1t01]], [[2b0h|2b0h]], [[2g35|2g35]], [[1zw3|1zw3]], [[1sj8|1sj8]], [[1sj7|1sj7]]</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]] 2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2x0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x0c OCA], [http://pdbe.org/2x0c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x0c RCSB], [http://www.ebi.ac.uk/pdbsum/2x0c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x0c 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=2x0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x0c OCA], [https://pdbe.org/2x0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x0c RCSB], [https://www.ebi.ac.uk/pdbsum/2x0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x0c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x0/2x0c_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x0/2x0c_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | ==See Also== | | ==See Also== |
| | *[[Talin|Talin]] | | *[[Talin|Talin]] |
| | + | *[[Talin 3D structures|Talin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Barsukov, I L]] | + | [[Category: Mus musculus]] |
| - | [[Category: Bate, N]] | + | [[Category: Barsukov IL]] |
| - | [[Category: Critchely, D R]] | + | [[Category: Bate N]] |
| - | [[Category: Emsley, J]] | + | [[Category: Critchely DR]] |
| - | [[Category: Gingras, A R]] | + | [[Category: Emsley J]] |
| - | [[Category: Goult, B T]] | + | [[Category: Gingras AR]] |
| - | [[Category: Actin]]
| + | [[Category: Goult BT]] |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Cell membrane]]
| + | |
| - | [[Category: Cell projection]]
| + | |
| - | [[Category: Cytoskeleton]]
| + | |
| - | [[Category: Integrin]]
| + | |
| - | [[Category: Synemin]]
| + | |
| - | [[Category: Vinculin]]
| + | |
| 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 an adaptor protein that couples integrins to F-actin. Structural studies show that the N-terminal talin head contains an atypical FERM domain while the N- and C-terminal parts of the talin rod comprise a series of alpha-helical bundles. However, determining the structure of the central part of the rod has proved problematic. Residues 1359-1659 are homologous to the MESDc1 gene product, and we therefore expressed this region of talin in E. coli. The crystal structure shows a unique fold comprised of a 5- and 4-helix bundle. The 5-helix bundle is composed of non-sequential helices due to insertion of the 4-helix bundle into the loop at the C-terminus of helix alpha3. The linker connecting the bundles forms a two-stranded anti-parallel beta-sheet likely limiting the relative movement of the two bundles. Because the 5-helix bundle contains the N- and C-termini of this module, we propose that it is linked by short loops to adjacent bundles while the 4-helix bundle protrudes from the rod. This suggests the 4-helix bundle has a unique role, and its pI (7.8) is higher than other rod domains. Both helical bundles contain vinculin-binding sites, but that in the isolated 5-helix bundle is cryptic whereas that in the isolated 4-helix bundle is constitutively active. In contrast, both bundles are required for actin binding. Finally, we show that the MESDc1 protein, which is predicted to have a similar fold, is a novel actin binding protein.
The central region of talin has a unique fold that binds vinculin and actin.,Gingras AR, Bate N, Goult BT, Patel B, Kopp PM, Emsley J, Barsukov IL, Roberts GC, Critchley DR J Biol Chem. 2010 Jul 7. PMID:20610383[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gingras AR, Bate N, Goult BT, Patel B, Kopp PM, Emsley J, Barsukov IL, Roberts GC, Critchley DR. The central region of talin has a unique fold that binds vinculin and actin. J Biol Chem. 2010 Jul 7. PMID:20610383 doi:10.1074/jbc.M109.095455
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