Selected article for: "amino acid and therapeutic antibody"
Author: Feng, Mingqian; Bian, Hejiao; Wu, Xiaolin; Fu, Tianyun; Fu, Ying; Hong, Jessica; Fleming, Bryan D; Flajnik, Martin F; Ho, Mitchell
Title: Construction and next-generation sequencing analysis of a large phage-displayed V(NAR) single-domain antibody library from six naïve nurse sharks
  • Document date: 2018_11_7
    • ID: wc6k06sm_15
    Snippet: In this study, we use two canonical cysteines located at both amino acid 21 and 82 as a key criterion to characterize Type I-IV V NAR families. About 5% of the total V NAR s do not fit in any one of the four known V NAR type families. We have identified ∼11% of the total V NAR s are classical Type I and 57% classical Type II. While a majority of the V NAR s are either classical Type I or Type II, ∼30% of the V NAR s do not fit any of the four.....
    Document: In this study, we use two canonical cysteines located at both amino acid 21 and 82 as a key criterion to characterize Type I-IV V NAR families. About 5% of the total V NAR s do not fit in any one of the four known V NAR type families. We have identified ∼11% of the total V NAR s are classical Type I and 57% classical Type II. While a majority of the V NAR s are either classical Type I or Type II, ∼30% of the V NAR s do not fit any of the four classical types. Most of these nonclassical V NAR s have various numbers of cysteines (Fig. 2) . Future structural and functional analysis of the binders isolated from the library for various antigens will be needed to understand the role of these non-classical V NAR s in therapeutic antibody discovery and engineering.

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