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6CA7

Crystal structure of PCT64_13C, a strain specific anti-HIV antibody

Summary for 6CA7
Entry DOI10.2210/pdb6ca7/pdb
Related5FEH 6CA6
DescriptorPCT64_13C light chain, PCT64_13C heavy chain (3 entities in total)
Functional Keywordsantibody, neutralizing, immune system
Biological sourceHomo sapiens
More
Total number of polymer chains2
Total formula weight48982.39
Authors
Murrell, S.,Wilson, I.A. (deposition date: 2018-01-29, release date: 2018-06-27, Last modification date: 2024-11-06)
Primary citationRantalainen, K.,Berndsen, Z.T.,Murrell, S.,Cao, L.,Omorodion, O.,Torres, J.L.,Wu, M.,Umotoy, J.,Copps, J.,Poignard, P.,Landais, E.,Paulson, J.C.,Wilson, I.A.,Ward, A.B.
Co-evolution of HIV Envelope and Apex-Targeting Neutralizing Antibody Lineage Provides Benchmarks for Vaccine Design.
Cell Rep, 23:3249-3261, 2018
Cited by
PubMed Abstract: Broadly neutralizing antibodies (bnAbs) targeting the HIV envelope glycoprotein (Env) typically take years to develop. Longitudinal analyses of both neutralizing antibody lineages and viruses at serial time points during infection provide a basis for understanding the co-evolutionary contest between HIV and the humoral immune system. Here, we describe the structural characterization of an apex-targeting antibody lineage and autologous clade A viral Env from a donor in the Protocol C cohort. Comparison of Ab-Env complexes at early and late time points reveals that, within the antibody lineage, the CDRH3 loop rigidifies, the bnAb angle of approach steepens, and surface charges are mutated to accommodate glycan changes. Additionally, we observed differences in site-specific glycosylation between soluble and full-length Env constructs, which may be important for tuning optimal immunogenicity in soluble Env trimers. These studies therefore provide important guideposts for design of immunogens that prime and mature nAb responses to the Env V2-apex.
PubMed: 29898396
DOI: 10.1016/j.celrep.2018.05.046
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.643 Å)
Structure validation

237735

數據於2025-06-18公開中

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