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 for ligand 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, a transmembrane domain and a cytoplasmic 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 is N-terminal to the I-like domain. Below the hybrid domain is the PSI domain, which completes the headpiece. The lower legs consist of EGF domains 1-4 and the β tail domain. Finally there is a transmembrane domain, and the C-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.
Guilliano MJ, Foxx-Orenstein AE, Lebman DA (Feb 2001). "The microenvironment of human Peyer's patches inhibits the increase in CD38 expression associated with the germinal center reaction". Journal of Immunology. 166 (4): 2179–85. doi:10.4049/jimmunol.166.4.2179. PMID11160270. S2CID36075610.
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