|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Cryo-EM structure of autoinhibited human talin-1== | | ==Cryo-EM structure of autoinhibited human talin-1== |
| - | <StructureSection load='6r9t' size='340' side='right'caption='[[6r9t]], [[Resolution|resolution]] 6.20Å' scene=''> | + | <SX load='6r9t' size='340' side='right' viewer='molstar' caption='[[6r9t]], [[Resolution|resolution]] 6.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6r9t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R9T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R9T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6r9t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6R9T FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TLN1, KIAA1027, TLN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.2Å</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=6r9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r9t OCA], [http://pdbe.org/6r9t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r9t RCSB], [http://www.ebi.ac.uk/pdbsum/6r9t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r9t 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=6r9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r9t OCA], [https://pdbe.org/6r9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r9t RCSB], [https://www.ebi.ac.uk/pdbsum/6r9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r9t ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TLN1_HUMAN TLN1_HUMAN]] 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 (By similarity). | + | [https://www.uniprot.org/uniprot/TLN1_HUMAN TLN1_HUMAN] 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 (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 18: |
Line 18: |
| | </div> | | </div> |
| | <div class="pdbe-citations 6r9t" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6r9t" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Talin 3D structures|Talin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Biertumpfel, C]] | + | [[Category: Biertumpfel C]] |
| - | [[Category: Dedden, D]] | + | [[Category: Dedden D]] |
| - | [[Category: Mizuno, N]] | + | [[Category: Mizuno N]] |
| - | [[Category: Schumacher, S]] | + | [[Category: Schumacher S]] |
| - | [[Category: Zacharias, M]] | + | [[Category: Zacharias M]] |
| - | [[Category: Actin]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Focal adhesion]]
| + | |
| - | [[Category: Signaling]]
| + | |
| - | [[Category: Vinculin]]
| + | |
| Structural highlights
Function
TLN1_HUMAN 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 (By similarity).
Publication Abstract from PubMed
Focal adhesions (FAs) are protein machineries essential for cell adhesion, migration, and differentiation. Talin is an integrin-activating and tension-sensing FA component directly connecting integrins in the plasma membrane with the actomyosin cytoskeleton. To understand how talin function is regulated, we determined a cryoelectron microscopy (cryo-EM) structure of full-length talin1 revealing a two-way mode of autoinhibition. The actin-binding rod domains fold into a 15-nm globular arrangement that is interlocked by the integrin-binding FERM head. In turn, the rod domains R9 and R12 shield access of the FERM domain to integrin and the phospholipid PIP2 at the membrane. This mechanism likely ensures synchronous inhibition of integrin, membrane, and cytoskeleton binding. We also demonstrate that compacted talin1 reversibly unfolds to an approximately 60-nm string-like conformation, revealing interaction sites for vinculin and actin. Our data explain how fast switching between active and inactive conformations of talin could regulate FA turnover, a process critical for cell adhesion and signaling.
The Architecture of Talin1 Reveals an Autoinhibition Mechanism.,Dedden D, Schumacher S, Kelley CF, Zacharias M, Biertumpfel C, Fassler R, Mizuno N Cell. 2019 Sep 19;179(1):120-131.e13. doi: 10.1016/j.cell.2019.08.034. PMID:31539492[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dedden D, Schumacher S, Kelley CF, Zacharias M, Biertumpfel C, Fassler R, Mizuno N. The Architecture of Talin1 Reveals an Autoinhibition Mechanism. Cell. 2019 Sep 19;179(1):120-131.e13. doi: 10.1016/j.cell.2019.08.034. PMID:31539492 doi:http://dx.doi.org/10.1016/j.cell.2019.08.034
|