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Article

Effects of a remote mutation from the contact paratope on the structure of CDR-H3 in the anti-HIV neutralizing antibody PG16.

Scientific reports - 27 Dec 2019

Kondo Hiroko X, Kiribayashi Ryo, Kuroda Daisuke, Kohda Jiro, Kugimiya Akimitsu, Nakano Yasuhisa, Tsumoto Kouhei, Takano Yu

Abstract excerpt

PG16 is a broadly neutralizing antibody to the human immunodeficiency virus (HIV). A crystal structure of PG16 revealed that the unusually long 28-residue complementarity determining region (CDR) H3 forms a unique subdomain, referred to as a "hammerhead", that directly contacts the antigen. The hammerhead apparently governs the function of PG16 while a previous experimental assay showed that the mutation of...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 31882602
DOI: 10.1038/s41598-019-56154-y
PMCID: PMC6934664

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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