3G9W

Crystal Structure of Talin2 F2-F3 in Complex with the Integrin Beta1D Cytoplasmic Tail

Summary for 3G9W

• Entry DOI: 10.2210/pdb3g9w/pdb
• Descriptor: Talin-2, Integrin beta-1D, GLYCEROL, ... (5 entities in total)
• Functional Keywords: protein-protein complex, ph domain superfold, ptb domain, helical bundle, intrinsically unstructured, cell adhesion
• Biological source: Mus musculus (mouse); More
• Cellular location: Cell junction, focal adhesion (By similarity): Q71LX4; Cell membrane; Single-pass type I membrane protein. Isoform 5: Cell membrane, sarcolemma (By similarity): P05556
• Total number of polymer chains: 4
• Total formula weight: 64670.16

Authors

Anthis, N.J.,Wegener, K.L.,Ye, F.,Kim, C.,Lowe, E.D.,Vakonakis, I.,Bate, N.,Critchley, D.R.,Ginsberg, M.H.,Campbell, I.D. (deposition date: 2009-02-15, release date: 2009-10-20, Last modification date: 2023-11-01)

Primary citation

Anthis, N.J.,Wegener, K.L.,Ye, F.,Kim, C.,Goult, B.T.,Lowe, E.D.,Vakonakis, I.,Bate, N.,Critchley, D.R.,Ginsberg, M.H.,Campbell, I.D.
The structure of an integrin/talin complex reveals the basis of inside-out signal transduction
Embo J., 28:3623-3632, 2009

PubMed Abstract: Fundamental to cell adhesion and migration, integrins are large heterodimeric membrane proteins that uniquely mediate inside-out signal transduction, whereby adhesion to the extracellular matrix is activated from within the cell by direct binding of talin to the cytoplasmic tail of the beta integrin subunit. Here, we report the first structure of talin bound to an authentic full-length beta integrin tail. Using biophysical and whole cell measurements, we show that a specific ionic interaction between the talin F3 domain and the membrane-proximal helix of the beta tail disrupts an integrin alpha/beta salt bridge that helps maintain the integrin inactive state. Second, we identify a positively charged surface on the talin F2 domain that precisely orients talin to disrupt the heterodimeric integrin transmembrane (TM) complex. These results show key structural features that explain the ability of talin to mediate inside-out TM signalling.

PubMed: 19798053
DOI: 10.1038/emboj.2009.287

Experimental method

X-RAY DIFFRACTION (2.165 Å)