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| | ==Solution structure of the talin F3 in complex with layilin cytodomain== | | ==Solution structure of the talin F3 in complex with layilin cytodomain== |
| - | <StructureSection load='2k00' size='340' side='right' caption='[[2k00]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2k00' size='340' side='right'caption='[[2k00]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2k00]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K00 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K00 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2k00]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K00 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TLN1, TLN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k00 OCA], [http://pdbe.org/2k00 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k00 RCSB], [http://www.ebi.ac.uk/pdbsum/2k00 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2k00 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=2k00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k00 OCA], [https://pdbe.org/2k00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k00 RCSB], [https://www.ebi.ac.uk/pdbsum/2k00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k00 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TLN1_CHICK TLN1_CHICK]] Probably involved in connections of major cytoskeletal structures to the plasma membrane. Talin is a high molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts. [[http://www.uniprot.org/uniprot/LAYN_MOUSE LAYN_MOUSE]] Receptor for hyaluronate (By similarity). | + | [https://www.uniprot.org/uniprot/TLN1_CHICK TLN1_CHICK] Probably involved in connections of major cytoskeletal structures to the plasma membrane. Talin is a 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: Gallus gallus]] | | [[Category: Gallus gallus]] |
| - | [[Category: Barsukov, I L]] | + | [[Category: Large Structures]] |
| - | [[Category: Wegener, K L]] | + | [[Category: Mus musculus]] |
| - | [[Category: Alternative splicing]] | + | [[Category: Barsukov IL]] |
| - | [[Category: Cell projection]] | + | [[Category: Wegener KL]] |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Cytoskeleton]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Lectin]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| Structural highlights
Function
TLN1_CHICK Probably involved in connections of major cytoskeletal structures to the plasma membrane. Talin is a 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 cytoskeletal protein that is involved in coupling the integrin family of cell adhesion molecules to the actin cytoskeleton, colocalising with the integrins in focal adhesions (FAs). However, at the leading edge of motile cells, talin colocalises with the hyaluronan receptor layilin in what are thought to be transient adhesions, some of which subsequently mature into more stable FAs. During this maturation process, layilin is replaced with integrins, which are highly clustered in FAs, where localised production of PI(4,5)P(2) by type 1 phosphatidyl inositol phosphate kinase type 1gamma (PIPK1gamma) is thought to play a role in FA assembly. The talin FERM F3 subdomain binds both the integrin beta-subunit cytoplasmic domain and PIPK1gamma, and these interactions are understood in detail at the atomic level. The talin F3 domain also binds to short sequences in the layilin cytoplasmic domain, and here we report the structure of the talin/layilin complex, which shows that talin binds integrins, PIPK1gamma and layilin in similar although subtly different ways. Based on structure comparisons, we designed a set of talin F3 mutations that selectively affected the affinity of talin for its targets, as determined by stopped-flow fluorescence measurements. Such mutations will help to assess the importance of the interactions between talin and its various ligands in cell adhesion and migration.
Structural basis for the interaction between the cytoplasmic domain of the hyaluronate receptor layilin and the talin F3 subdomain.,Wegener KL, Basran J, Bagshaw CR, Campbell ID, Roberts GC, Critchley DR, Barsukov IL J Mol Biol. 2008 Sep 26;382(1):112-26. Epub 2008 Jul 7. PMID:18638481[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wegener KL, Basran J, Bagshaw CR, Campbell ID, Roberts GC, Critchley DR, Barsukov IL. Structural basis for the interaction between the cytoplasmic domain of the hyaluronate receptor layilin and the talin F3 subdomain. J Mol Biol. 2008 Sep 26;382(1):112-26. Epub 2008 Jul 7. PMID:18638481 doi:10.1016/j.jmb.2008.06.087
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