Cryo-EM structures of full-length integrin αIIbβ3 in native lipids
Cryo-EM structures of full-length integrin αIIbβ3 in native lipids
About this item
Full title
Author / Creator
Publisher
London: Nature Publishing Group UK
Journal title
Language
English
Formats
Publication information
Publisher
London: Nature Publishing Group UK
Subjects
More information
Scope and Contents
Contents
Platelet integrin αIIbβ3 is maintained in a bent inactive state (low affinity to physiologic ligand), but can rapidly switch to a ligand-competent (high-affinity) state in response to intracellular signals (“inside-out” activation). Once bound, ligands drive proadhesive “outside-in” signaling. Anti-αIIbβ3 drugs like eptifibatide can engage the inac...
Alternative Titles
Full title
Cryo-EM structures of full-length integrin αIIbβ3 in native lipids
Authors, Artists and Contributors
Author / Creator
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_b492d27f5ecf4a52879de123c3081790
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_b492d27f5ecf4a52879de123c3081790
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-023-39763-0