Structures of the platelet calcium- and integrin-binding protein and the alphaIIb-integrin cytoplasmic domain suggest a mechanism for calcium-regulated recognition; homology modelling and NMR studies.
Hwang, P M; Vogel, H J.
J Mol Recognit
; 13(2): 83-92, 2000 Mar-Apr.
Artigo em Inglês | MEDLINE | ID: mdl-10822252
A new view of integrin αIIbß3 bound to membrane.
Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces.
The Structure of a Full-length Membrane-embedded Integrin Bound to a Physiological Ligand.
The structure of a receptor with two associating transmembrane domains on the cell surface: integrin alphaIIbbeta3.
Three-dimensional reconstruction of intact human integrin αIIbß3: new implications for activation-dependent ligand binding.
Metadynamics Simulations Rationalise the Conformational Effects Induced by N-Methylation of RGD Cyclic Hexapeptides.
Intermolecular transmembrane domain interactions activate integrin αIIbß3.
Autonomous conformational regulation of ß<sub>3</sub> integrin and the conformation-dependent property of HPA-1a alloantibodies.
Integrin αIIbß3 inside-out activation: an in situ conformational analysis reveals a new mechanism.
Three-Dimensional Structures of Full-Length, Membrane-Embedded Human α(IIb)ß(3) Integrin Complexes.