9p98 | pdb_00009p98

CryoEM structure of the open integrin alphaEbeta7 bound to fab LF61

spinqualitylabelsall models 9p98, resolution 2.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9p98 is a 4 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.93Å Ligands: BMA, CA, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ITAE_HUMAN Integrin alpha-E/beta-7 is a receptor for E-cadherin. It mediates adhesion of intra-epithelial T-lymphocytes to epithelial cell monolayers. Publication Abstract from PubMed Integrins bind ligands between their alpha (alpha) and beta (beta) subunits and transmit signals through conformational changes. Early in chordate evolution, some alpha subunits acquired an "inserted" (I) domain that expanded integrin's ligand-binding repertoire but obstructed the ancestral ligand pocket, seemingly blocking conventional integrin activation. Here, we compare cryo-electron microscopy structures of apo and ligand-bound states of the I domain-containing alphaEbeta(7) integrin and the I domain-lacking alpha(4)beta(7) integrin to illuminate how the I domain intrinsically mimics an extrinsic ligand to preserve integrin function. We trace the I domain's evolutionary origin to an ancestral collagen-collagen interaction domain, identifying an ancient molecular exaptation that facilitated integrin activation immediately upon I domain insertion. Our analyses reveal the evolutionary and biochemical basis of expanded cellular communication in vertebrates. Molecular exaptation by the integrin alphaI domain.,Hollis JA, Chan MC, Malik HS, Campbell MG Sci Adv. 2025 Sep 12;11(37):eadx9567. doi: 10.1126/sciadv.adx9567. Epub 2025 Sep , 10. PMID:40929264 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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