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1S4X

NMR Structure of the integrin B3 cytoplasmic domain in DPC micelles

Summary for 1S4X
Entry DOI10.2210/pdb1s4x/pdb
Related1S4W
DescriptorIntegrin beta-3 (1 entity in total)
Functional Keywordscell adhesion
Biological sourceHomo sapiens (human)
Cellular locationMembrane; Single-pass type I membrane protein: P05106
Total number of polymer chains1
Total formula weight7757.64
Authors
Vinogradova, O.,Vaynberg, J.,Kong, X.,Haas, T.A.,Plow, E.F.,Qin, J. (deposition date: 2004-01-19, release date: 2004-03-09, Last modification date: 2024-05-22)
Primary citationVinogradova, O.,Vaynberg, J.,Kong, X.,Haas, T.A.,Plow, E.F.,Qin, J.
Membrane-mediated structural transitions at the cytoplasmic face during integrin activation.
Proc.Natl.Acad.Sci.USA, 101:4094-4099, 2004
Cited by
PubMed Abstract: Cytoplasmic face-mediated integrin inside-out activation remains a paradigm in transmembrane signal transduction. Emerging evidence suggests that this process involves dissociation of the complex between the integrin cytoplasmic tails; however, a dynamic image of how it occurs on the membrane surface remains elusive. We show here that, whereas membrane-proximal helices of integrin alpha/beta cytoplasmic tails associate in cytoplasm-like aqueous medium, they become partially embedded into membrane-mimetic micelles when unclasped. Membrane embedding induces substantial structural changes of the cytoplasmic tails as compared to their aqueous conformations and suggests there may be an upward movement of the membrane-proximal helices into the membrane during their separation. We further demonstrate that the beta3 tail exhibits additional membrane binding site at its C terminus containing the NPLY motif. Talin, a key intracellular integrin activator, recognizes this site as well as the membrane-proximal helix, thereby promoting cytoplasmic tail separation along the membrane surface. These data provide a structural basis of membrane-mediated changes at the cytoplasmic face in regulating integrin activation and signaling.
PubMed: 15024114
DOI: 10.1073/pnas.0400742101
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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