Abstract
Activation of integrins, transmebrane receptors that mediate cell adhesion and cell migration, is accompanied by a series of conformational rearrangements resulting in changes in affinity and avidity. Several observations indicate that conformational changes induced by ligand interaction with integrins lead to exchange of disulfide bonds within the integrin molecule, which stabilizes the altered conformation. Closely spaced thiols in proteins that interconvert between the dithiol form and disulfide bonds are called vicinal thiols.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
