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© Research
Publication : Journal of structural biology

Structural studies on full-length talin1 reveal a compact auto-inhibited dimer: implications for talin activation.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of structural biology - 01 Oct 2013

Goult BT, Xu XP, Gingras AR, Swift M, Patel B, Bate N, Kopp PM, Barsukov IL, Critchley DR, Volkmann N, Hanein D,

Link to Pubmed [PMID] – 23726984

Link to DOI – 10.1016/j.jsb.2013.05.014S1047-8477(13)00146-9

J Struct Biol 2013 Oct; 184(1): 21-32

Talin is a large adaptor protein that activates integrins and couples them to cytoskeletal actin. Talin contains an N-terminal FERM (band 4.1, ezrin, radixin, moesin) domain (the head) linked to a flexible rod comprised of 13 amphipathic helical bundles (R1-R13) that terminate in a C-terminal helix (DD) that forms an anti-parallel dimer. We derived a three-dimensional structural model of full-length talin at a resolution of approximately 2.5nm using EM reconstruction of full-length talin and the known shapes of the individual domains and inter-domain angles as derived from small angle X-ray scattering. Talin adopts a compact conformation consistent with a dimer in which the two talin rods form a donut-shaped structure, with the two talin heads packed side by side occupying the hole at the center of this donut. In this configuration, the integrin binding site in the head domain and the actin-binding site at the carboxy-terminus of the rod are masked, implying that talin must unravel before it can support integrin activation and engage the actin cytoskeleton.

https://pubmed.ncbi.nlm.nih.gov/23726984