2K9J

Integrin alphaIIb-beta3 transmembrane complex

Summary for 2K9J

• Entry DOI: 10.2210/pdb2k9j/pdb
• Related: 2RMZ 2k1a
• NMR Information: BMRB: 16497
• Descriptor: Integrin alpha-IIb light chain, Integrin beta-3 (2 entities in total)
• Functional Keywords: integrin, transmembrane complex, cell adhesion, cleavage on pair of basic residues, disease mutation, glycoprotein, pyrrolidone carboxylic acid, receptor, host-virus interaction, phosphoprotein, membrane protein
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P08514 P05106
• Total number of polymer chains: 2
• Total formula weight: 9464.62

Authors

Lau, T.,Kim, C.,Ginsberg, M.H.,Ulmer, T.S. (deposition date: 2008-10-15, release date: 2009-03-24, Last modification date: 2024-05-22)

Primary citation

Lau, T.L.,Kim, C.,Ginsberg, M.H.,Ulmer, T.S.
The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling
Embo J., 28:1351-1361, 2009

PubMed Abstract: Heterodimeric integrin adhesion receptors regulate cell migration, survival and differentiation in metazoa by communicating signals bi-directionally across the plasma membrane. Protein engineering and mutagenesis studies have suggested that the dissociation of a complex formed by the single-pass transmembrane (TM) segments of the alpha and beta subunits is central to these signalling events. Here, we report the structure of the integrin alphaIIbbeta3 TM complex, structure-based site-directed mutagenesis and lipid embedding estimates to reveal the structural event that underlies the transition from associated to dissociated states, that is, TM signalling. The complex is stabilized by glycine-packing mediated TM helix crossing within the extracellular membrane leaflet, and by unique hydrophobic and electrostatic bridges in the intracellular leaflet that mediate an unusual, asymmetric association of the 24- and 29-residue alphaIIb and beta3 TM helices. The structurally unique, highly conserved integrin alphaIIbbeta3 TM complex rationalizes bi-directional signalling and represents the first structure of a heterodimeric TM receptor complex.

PubMed: 19279667
DOI: 10.1038/emboj.2009.63

Experimental method

SOLUTION NMR