1M8O

Platelet integrin alfaIIb-beta3 cytoplasmic domain

Summary for 1M8O

• Entry DOI: 10.2210/pdb1m8o/pdb
• Descriptor: platelet integrin alfaIIb subunit: cytoplasmic domain, platelet integrin beta3 subunit: cytoplasmic domain (2 entities in total)
• Functional Keywords: alfa helix, platelet, 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: 7981.85

Authors

Vinogradova, O.,Velyvis, A.,Velyviene, A.,Hu, B.,Haas, T.,Plow, E.F.,Qin, J. (deposition date: 2002-07-25, release date: 2002-09-18, Last modification date: 2024-05-22)

Primary citation

Vinogradova, O.,Velyvis, A.,Velyviene, A.,Hu, B.,Haas, T.A.,Plow, E.F.,Qin, J.
A Structural mechanism of integrin alfaiib beta3 "Inside-out" Activation as regulated by its cytoplasmic face.
Cell(Cambridge,Mass.), 110:587-597, 2002

PubMed Abstract: Activation of the ligand binding function of integrin heterodimers requires transmission of an "inside-out" signal from their small intracellular segments to their large extracellular domains. The structure of the cytoplasmic domain of a prototypic integrin alpha(IIb)beta(3) has been solved by NMR and reveals multiple hydrophobic and electrostatic contacts within the membrane-proximal helices of its alpha and the beta cytoplasmic tails. The interface interactions are disrupted by point mutations or the cytoskeletal protein talin that are known to activate the receptor. These results provide a structural mechanism by which a handshake between the alpha and the beta cytoplasmic tails restrains the integrin in a resting state and unclasping of this interaction triggers the inside-out conformational signal that leads to receptor activation.

PubMed: 12230976
DOI: 10.1016/S0092-8674(02)00906-6

Experimental method

SOLUTION NMR