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Publication Abstract from PubMed

OBJECTIVE: To determine the X-ray structure and biophysical properties of a Camelid VHH isolated from a naive phage display library. RESULTS: Single domain antibodies (VHH) derived from the unique immune system of the Camelidae family have gained traction as useful tools for biotechnology as well as a source of potentially novel therapeutics. Here we report the structure and biophysical characterization of a VHH originally isolated from a naive camelid phage display library. VHH R419 has a melting temperate of 66 degrees C and was found to be a monomer in solution. The protein crystallized in space group P6522 and the structure was solved by molecular replacement to a resolution of 1.5 A. The structure revealed a flat paratope with CDR loops that could be classified into existing canonical loop structures. A combination of high expression yield, stability and rapid crystallization might make R419 into a candidate scaffold for CDR grafting and homology modeling.

Structure of a VHH isolated from a naive phage display library.,White B, Huh I, Brooks CL BMC Res Notes. 2019 Mar 19;12(1):154. doi: 10.1186/s13104-019-4197-0. PMID:30890176^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.