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• W2125435732 abstract "We used integrin αLβ2 heterodimers containing I domains locked open (active) or closed (inactive) with disulfide bonds to investigate regulatory interactions among domains in integrins. mAbs to the αL I domain and β2 I-like domain inhibit adhesion of wild-type αLβ2 to intercellular adhesion molecule-1. However, with αLβ2 containing a locked open I domain, mAbs to the I domain were subdivided into subsets ( i ) that did not inhibit, and thus appear to inhibit by favoring the closed conformation, and ( ii ) that did inhibit, and thus appear to bind to the ligand binding site. Furthermore, αLβ2 containing a locked open I domain was completely resistant to inhibition by mAbs to the β2 I-like domain, but became fully susceptible to inhibition after disulfide reduction with DTT. This finding suggests that the I-like domain indirectly contributes to ligand binding by regulating opening of the I domain in wild-type αLβ2. Conversely, locking the I domain closed partially restrained conformational change of the I-like domain by Mn 2+ , as measured with mAb m24, which we map here to the β2 I-like domain. By contrast, locking the I domain closed or open did not affect constitutive or Mn 2+ -induced exposure of the KIM127 epitope in the β2 stalk region. Furthermore, locked open I domains, in αLβ2 complexes or expressed in isolation on the cell surface, bound to intercellular adhesion molecule-1 equivalently in Mg 2+ and Mn 2+ . These results suggest that Mn 2+ activates αLβ2 by binding to a site other than the I domain, most likely the I-like domain of β2." @default.
• W2125435732 created "2016-06-24" @default.
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• W2125435732 creator A5053036995 @default.
• W2125435732 date "2001-02-27" @default.
• W2125435732 modified "2023-09-23" @default.
• W2125435732 title "Locking in alternate conformations of the integrin αLβ2 I domain with disulfide bonds reveals functional relationships among integrin domains" @default.
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• W2125435732 doi "https://doi.org/10.1073/pnas.041618598" @default.
• W2125435732 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/30149" @default.
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