Structure of a VHH isolated from a naive phage display library

被引：7

作者：

White, Brandy ^{[1
]}

Huh, Ian ^{[1
]}

Brooks, Cory L. ^{[1
]}

机构：

[1] Calif State Univ Fresno, Dept Chem, 2555 E San Ramon Ave, Fresno, CA 93740 USA

来源：

BMC RESEARCH NOTES | 2019年 / 12卷 / 1期

基金：

美国国家卫生研究院;

关键词：

Nanobody; Single domain antibody; VHH;

D O I：

10.1186/s13104-019-4197-0

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 P6(5)22 and the structure was solved by molecular replacement to a resolution of 1.5 angstrom. 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.

引用

页数：6

共 22 条

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