The diversity of H3 loops determines the antigen-binding tendencies of antibody CDR loops-Reference-Cited by-同舟云学术

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The diversity of H3 loops determines the antigen-binding tendencies of antibody CDR loops

Published:2016-01-20 Issue:4 Volume:25 Page:815-825
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Tsuchiya Yuko¹,Mizuguchi Kenji¹

Affiliation:

1. National Institutes of Biomedical Innovation; Health and Nutrition; 7-6-8 Saito-Asagi Ibaraki Osaka 567-0085 Japan

Funder

Japan Society for the Promotion of Science (Grants-in-Aid for Scientific Research)

Japan Agency for Medical Research and Development (“The adjuvant database project”) to K.M

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2874/fullpdf

Reference28 articles.

1. Standard conformations for the canonical structures of immunoglobulins;Al-Lazikani;J Mol Biol,1997

2. A systematic comparison of free and bound antibodies reveals binding-related conformational changes;Sela-Culang;J Immunol,2012

3. Identification of specificity-determining residues in antibodies;Padlan;Faseb J,1995

4. The indistinguishability of epitopes from protein surface is explained by the distinct binding preferences of each of the six antigen-binding loops;Kunik;Protein Eng Des Sel,2013

5. Conformations of immunoglobulin hypervariable regions;Chothia;Nature,1989

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