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Structural basis for integrin bi-directional signaling
Author:        Updatetime:2011-10-31 Printer      Text Size:A A A 

Presenter: Jieqing Zhu, Associate Investigator

University: Medical College of Wisconsin

Time: 10:00-11:00, October 31, 2011

Venue: A203, Institute of Microbiology, Chinese Academy of Sciences

Abstract: Integrins are heterodimeric cell surface receptors that play important roles in cell-cell and cell-matrix adhesion. Integrins transmit signals bidirectionally across the cell membrane. Recent structural and biochemical studies have revealed that integrin activation is associated with a series of conformational rearrangements of extracellular, transmembrane, and cytoplasmic domains upon agonist stimulation inside the cell, or ligand binding outside the cell. The global conformational changes of integrin extracellular domains are characterized by changing from a compact bent conformation into an extended conformation with the separation of integrin headpiece and tailpiece interface. The integrin headpiece changes from a closed to an open configuration upon ligand binding. In this presentation, I will talk about my recent studies on structure and function of platelet specific integrinαIIbβ3, which is essential for hemostasis and thrombosis. I will show the structural characters of integrin ectodomain and transmembrane domain and how small RGD-like ligand induce integrin conformational change.These studies have very important implications for designing new type of integrin antagonists for therapeutic purpose.

 
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