Like all integrin subunits, β7 is a highly flexible, membrane-bound, extracellular protein that must pair with an α subunit for stability. The molecule's flexibility allows it to dynamically regulate its affinity forligand through conformational changes.[8] Beginning with the apical end of the protein, farthest from the cell membrane, the β7 is composed of a head and upper legs, collectively known as the headpiece, lower legs, atransmembrane domain and acytoplasmic tail. The top of the head is the I-like domain, sometimes called the βI domain, which, in combination with the α subunit, binds ligand. Just below this is the hybrid domain, a portion of which isN-terminal to the I-like domain. Below the hybrid domain is the PSI domain, which completes the headpiece. The lower legs consist ofEGF domains 1-4 and the β tail domain. Finally there is a transmembrane domain, and theC-terminal cytoplasmic tail.[9]
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Yuan QA, Jiang WM, Krissansen GW, Watson JD (1991). "Cloning and sequence analysis of a novel beta 2-related integrin transcript from T lymphocytes: homology of integrin cysteine-rich repeats to domain III of laminin B chains".International Immunology.2 (11):1097–108.doi:10.1093/intimm/2.11.1097.PMID2083230.
Erle DJ, Brown T, Christian D, Aris R (Mar 1994). "Lung epithelial lining fluid T cell subsets defined by distinct patterns of beta 7 and beta 1 integrin expression".American Journal of Respiratory Cell and Molecular Biology.10 (3):237–44.doi:10.1165/ajrcmb.10.3.7509610.PMID7509610.
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