1u89

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of VBS2 fragment of talin

Structural highlights

1u89 is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

The cytoskeletal protein talin plays a key role in activating integrins and in coupling them to the actin cytoskeleton. Its N-terminal globular head, which binds beta integrins, is linked to an extended rod having a C-terminal actin binding site and several vinculin binding sites (VBSs). The NMR structure of residues 755-889 of the rod (containing a VBS) is shown to be an amphipathic four-helix bundle with a left-handed topology. A talin peptide corresponding to the VBS binds the vinculin head; the X-ray crystallographic structure of this complex shows that the residues which interact with vinculin are buried in the hydrophobic core of the talin fragment. NMR shows that the interaction involves a major structural change in the talin fragment, including unfolding of one of its helices, making the VBS accessible to vinculin. Interestingly, the talin 755-889 fragment binds more than one vinculin head molecule, suggesting that the talin rod may contain additional as yet unrecognized VBSs.

A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head.,Fillingham I, Gingras AR, Papagrigoriou E, Patel B, Emsley J, Critchley DR, Roberts GC, Barsukov IL Structure. 2005 Jan;13(1):65-74. PMID:15642262^[1]

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

References

↑ Fillingham I, Gingras AR, Papagrigoriou E, Patel B, Emsley J, Critchley DR, Roberts GC, Barsukov IL. A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head. Structure. 2005 Jan;13(1):65-74. PMID:15642262 doi:10.1016/j.str.2004.11.006

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u89"

@@ Line 1: / Line 1: @@
 ==Solution structure of VBS2 fragment of talin==
-<StructureSection load='1u89' size='340' side='right'caption='[[1u89]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1u89' size='340' side='right'caption='[[1u89]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1u89]] is a 1 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=1U89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U89 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1u89]] is a 1 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=1U89 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U89 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;'>[[1sj7|1sj7]], [[1sj8|1sj8]]</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1u89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u89 OCA], [https://pdbe.org/1u89 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u89 RCSB], [https://www.ebi.ac.uk/pdbsum/1u89 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u89 ProSAT]</span></td></tr>
 </table>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Talin|Talin]]
+*[[Talin 3D structures|Talin 3D structures]]
 == References ==
 <references/>
@@ Line 36: / Line 36: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Barsukov, I L]]
+[[Category: Barsukov IL]]
-[[Category: Critchley, D R]]
+[[Category: Critchley DR]]
-[[Category: Emsley, J]]
+[[Category: Emsley J]]
-[[Category: Fillingham, I]]
+[[Category: Fillingham I]]
-[[Category: Gingras, A R]]
+[[Category: Gingras AR]]
-[[Category: Papagrigoriou, E]]
+[[Category: Papagrigoriou E]]
-[[Category: Patel, B]]
+[[Category: Patel B]]
-[[Category: Roberts, G C.K]]
+[[Category: Roberts GCK]]
-[[Category: 4-helix bundle]]
-[[Category: Left-handed]]
-[[Category: Structural protein]]

1u89

From Proteopedia

Current revision

Solution structure of VBS2 fragment of talin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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