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Here, we present the structures of several high-affinity inhibitory nanobodies, each bound to Cif. Comparison reveals two classes of nanobodies with distinct CDR sequences and convergent recognition strategies. Mimicry between CDR3 and CDR2 loops positions an aromatic residue for insertion through the active-site gate, accessing a cryptic epitope, which sterically blocks substrate access and provides an anchor point for high-affinity engagement. Projection of either inhibitory CDR toward the active-site entrance requires a relative 90\u00b0 rotation of the core immunoglobulin domain, and yet both classes engage the same set of stereochemical handholds within a highly overlapping shared epitope. The structurally distinct paratopes thus represent fundamentally distinct solutions, reflecting the remarkable capacity of the immune system to solve highly constrained molecular recognition challenges.\n                <\/jats:p>","DOI":"10.64898\/2026.02.09.704437","type":"posted-content","created":{"date-parts":[[2026,2,11]],"date-time":"2026-02-11T05:20:56Z","timestamp":1770787256000},"source":"Crossref","is-referenced-by-count":0,"title":["Convergent strategies for nanobody-mediated inhibition of an epoxide hydrolase"],"prefix":"10.64898","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8175-1196","authenticated-orcid":false,"given":"Adam R.","family":"Simard","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, New Hampshire, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8783-120X","authenticated-orcid":false,"given":"Noor 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