Structure and allosteric regulation of the αXβ2 integrin I domain

Thomas Vorup-Jensen, Christian Ostermeier, Motomu Shimaoka, Ulrich Hommel, Timothy A. Springer*

*Corresponding author for this work

    Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

    69 Citations (Scopus)


    The integrin αXβ2 (CD11c/CD18, p150,95) binds ligands through the I domain of the αX subunit. Ligands include the complement factor fragment iC3b, a key component in the innate immune defense, which, together with the expression of αXβ2 on dendritic cells and on other leukocytes, suggests a role in the immune response. We now report the structure of the αX I domain resolved at 1.65 Å by x-ray crystallography. To analyze structural requirements for ligand binding we made a mutation in the αX I domain C-terminal helix, which increased the affinity for iC3b ≈200-fold to 2.4 μM compared with the wild-type domain affinity of ≈400 μM. Gel permeation chromatography supported a conformational change between the wild-type and mutated domains. Conservation of allosteric regulation in the αX I domain points to the functional importance of this phenomenon.

    Original languageEnglish
    JournalProceedings of the National Academy of Sciences
    Pages (from-to)1873-1878
    Number of pages6
    Publication statusPublished - 18 Feb 2003


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