1mix: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mix]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MIX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MIX FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mix]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MIX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MIX FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1miz|1miz]], [[1mk7|1mk7]], [[1mk9|1mk9]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1miz|1miz]], [[1mk7|1mk7]], [[1mk9|1mk9]]</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mix OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mix RCSB], [http://www.ebi.ac.uk/pdbsum/1mix PDBsum]</span></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=1mix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mix OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mix RCSB], [http://www.ebi.ac.uk/pdbsum/1mix PDBsum]</span></td></tr>
<table>
</table>
== 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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Calderwood, D A.]]
[[Category: Calderwood, D A]]
[[Category: Campbell, I D.]]
[[Category: Campbell, I D]]
[[Category: Critchley, D.]]
[[Category: Critchley, D]]
[[Category: Garcia-Alvarez, B.]]
[[Category: Garcia-Alvarez, B]]
[[Category: Ginsberg, M H.]]
[[Category: Ginsberg, M H]]
[[Category: Liddington, R C.]]
[[Category: Liddington, R C]]
[[Category: Pereda, J M.de.]]
[[Category: Pereda, J M.de]]
[[Category: Ulmer, T S.]]
[[Category: Ulmer, T S]]
[[Category: Cytoskeleton]]
[[Category: Cytoskeleton]]
[[Category: Ferm domain]]
[[Category: Ferm domain]]

Revision as of 09:37, 25 December 2014

Crystal structure of a FERM domain of TalinCrystal structure of a FERM domain of Talin

Structural highlights

1mix is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, RCSB, PDBsum

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

The binding of cytoplasmic proteins, such as talin, to the cytoplasmic domains of integrin adhesion receptors mediates bidirectional signal transduction. Here we report the crystal structure of the principal integrin binding and activating fragment of talin, alone and in complex with fragments of the beta 3 integrin tail. The FERM (four point one, ezrin, radixin, and moesin) domain of talin engages integrins via a novel variant of the canonical phosphotyrosine binding (PTB) domain-NPxY ligand interaction that may be a prototype for FERM domain recognition of transmembrane receptors. In combination with NMR and mutational analysis, our studies reveal the critical interacting elements of both talin and the integrin beta 3 tail, providing structural paradigms for integrin linkage to the cell interior.

Structural determinants of integrin recognition by talin.,Garcia-Alvarez B, de Pereda JM, Calderwood DA, Ulmer TS, Critchley D, Campbell ID, Ginsberg MH, Liddington RC Mol Cell. 2003 Jan;11(1):49-58. PMID:12535520[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Garcia-Alvarez B, de Pereda JM, Calderwood DA, Ulmer TS, Critchley D, Campbell ID, Ginsberg MH, Liddington RC. Structural determinants of integrin recognition by talin. Mol Cell. 2003 Jan;11(1):49-58. PMID:12535520

1mix, resolution 1.75Å

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OCA