Unknown

Dataset Information

0

The Structure of a Full-length Membrane-embedded Integrin Bound to a Physiological Ligand.


ABSTRACT: Increased ligand binding to integrin ("activation") underpins many biological processes, such as leukocyte trafficking, cell migration, host-pathogen interaction, and hemostasis. Integrins exist in several conformations, ranging from compact and bent to extended and open. However, the exact conformation of membrane-embedded, full-length integrin bound to its physiological macromolecular ligand is still unclear. Integrin ?IIb?3, the most abundant integrin in platelets, has been a prototype for integrin activation studies. Using negative stain electron microscopy and nanodisc-embedding to provide a membrane-like environment, we visualized the conformation of full-length ?IIb?3 in both a Mn(2+)-activated, ligand-free state and a Mn(2+)-activated, fibrin-bound state. Activated but ligand-free integrins exist mainly in the compact conformation, whereas fibrin-bound ?IIb?3 predominantly exists in a fully extended, headpiece open conformation. Our results show that membrane-embedded, full-length integrin adopts an extended and open conformation when bound to its physiological macromolecular ligand.

SUBMITTER: Dai A 

PROVIDER: S-EPMC4646401 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

The Structure of a Full-length Membrane-embedded Integrin Bound to a Physiological Ligand.

Dai Aguang A   Ye Feng F   Taylor Dianne W DW   Hu Guiqing G   Ginsberg Mark H MH   Taylor Kenneth A KA  

The Journal of biological chemistry 20150921 45


Increased ligand binding to integrin ("activation") underpins many biological processes, such as leukocyte trafficking, cell migration, host-pathogen interaction, and hemostasis. Integrins exist in several conformations, ranging from compact and bent to extended and open. However, the exact conformation of membrane-embedded, full-length integrin bound to its physiological macromolecular ligand is still unclear. Integrin αIIbβ3, the most abundant integrin in platelets, has been a prototype for in  ...[more]

Similar Datasets

| S-EPMC4776043 | biostudies-literature
| S-EPMC4663128 | biostudies-literature
| S-EPMC6428961 | biostudies-literature
| S-EPMC5732763 | biostudies-literature
| EMPIAR-10977 | biostudies-other
| EMPIAR-10978 | biostudies-other
| S-EPMC5071624 | biostudies-literature
| S-EPMC7058448 | biostudies-literature
| S-EPMC3756332 | biostudies-literature
| S-EPMC1852833 | biostudies-literature