Ontology highlight
ABSTRACT:
SUBMITTER: Li J
PROVIDER: S-EPMC5331762 | biostudies-literature | 2017 Mar
REPOSITORIES: biostudies-literature
Li Jing J Su Yang Y Xia Wei W Qin Yan Y Humphries Martin J MJ Vestweber Dietmar D Cabañas Carlos C Lu Chafen C Springer Timothy A TA
The EMBO journal 20170125 5
We show that the three conformational states of integrin α<sub>5</sub>β<sub>1</sub> have discrete free energies and define activation by measuring intrinsic affinities for ligand of each state and the equilibria linking them. The 5,000-fold higher affinity of the extended-open state than the bent-closed and extended-closed states demonstrates profound regulation of affinity. Free energy requirements for activation are defined with protein fragments and intact α<sub>5</sub>β<sub>1</sub> On the su ...[more]