6om1

Crystal structure of an atypical integrin

spinqualitylabelsall models 6om1, resolution 2.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6om1 is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.66Å Ligands: BMA, CA, EDO, MAN, MES, MG, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Integrin alphaVbeta8, which like alphaVbeta6 functions to activate TGF-betas, is atypical. Its beta8 subunit binds to a distinctive cytoskeleton adaptor and does not exhibit large changes in conformation upon binding to ligand. Here, crystal structures, hydrogen-deuterium exchange dynamics, and affinity measurements on mutants are used to compare alphaVbeta8 and alphaVbeta6. Lack of a binding site for one of three betaI domain divalent cations and a unique beta6-alpha7 loop conformation in beta8 facilitate movements of the alpha1 and alpha1' helices at the ligand binding pocket toward the high affinity state, without coupling to beta6-alpha7 loop reshaping and alpha7-helix pistoning that drive large changes in betaI domain-hybrid domain orientation seen in other integrins. Reciprocal swaps between beta6 and beta8 betaI domains increase affinity of alphaVbeta6 and decrease affinity of alphaVbeta8 and define features that regulate affinity of the betaI domain and its coupling to the hybrid domain. General structural features that regulate integrin affinity revealed by atypical alphaVbeta8.,Wang J, Su Y, Iacob RE, Engen JR, Springer TA Nat Commun. 2019 Dec 2;10(1):5481. doi: 10.1038/s41467-019-13248-5. PMID:31792290 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Integrin 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA