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Evidence for hetero‐association of transmembrane helices of integrins
Author(s) -
Gottschalk Kay-Eberhard,
Kessler Horst
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01443-1
Subject(s) - integrin , transmembrane protein , transmembrane domain , microbiology and biotechnology , protein subunit , cell surface receptor , extracellular , cytoplasm , signal transduction , cell membrane , biophysics , membrane protein , biology , chemistry , receptor , cell , membrane , biochemistry , gene
Integrins are important transmembrane cell‐surface receptors, which mediate interactions of the cell with other cells or the extracellular matrix. Integrins are heterodimers composed of an α‐ and a β‐subunit. They can switch between different activation states depending on intra‐ or extracellular signals. Inside/out and outside/in signaling is mediated via integrins across the membrane. A biologically important and yet still unanswered question is the role of the transmembrane domains in the signaling event. Here it is shown by simulated annealing/molecular dynamics calculations that recently published structural data of the cytoplasmic domains of integrin αIIbβ3 are supporting a structure with interacting transmembrane helices. This corroborates a model of transmembrane domains that are actively involved in the transmembrane signaling event.