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Article

Mutation of a conserved asparagine in the I-like domain promotes constitutively active integrins alphaLbeta2 and alphaIIbbeta3.

The Journal of biological chemistry - 22 Jun 2007

Cheng Ming, Foo Shen-Yun, Shi Min-Long, Tang Ren-Hong, Kong Le-Sheng, Law S K Alex, Tan Suet-Mien

Abstract excerpt

The leukocyte beta2 integrins are heterodimeric adhesion receptors required for a functional immune system. Many leukocyte adhesion deficiency-1 (LAD-1) mutations disrupt the expression and function of beta2 integrins. Herein, we further characterized the LAD-1 mutation N329S in the beta2 inserted (I)-like domain. This mutation converted alphaLbeta2 from a resting into a high affinity conformer because...

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Identifiers

PMID: 17468108
DOI: 10.1074/jbc.M701386200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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