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Conformational equilibria and intrinsic affinities define integrin activation
We show that the three conformational states of integrin α(5)β(1) 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‐...
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| Gepubliceerd in: | EMBO J |
|---|---|
| Hoofdauteurs: | , , , , , , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
John Wiley and Sons Inc.
2017
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5331762/ https://ncbi.nlm.nih.gov/pubmed/28122868 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.15252/embj.201695803 |
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