Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural basis for HIV-1 neutralization by 2F5-like antibodies m66 and m66.6.

Journal of virology - 1 Mar 2014

Ofek Gilad, Zirkle Brett, Yang Yongping, Zhu Zhongyu, McKee Krisha, Zhang Baoshan, Chuang Gwo-Yu, Georgiev Ivelin S, O'Dell Sijy, Doria-Rose Nicole, Mascola John R, Dimitrov Dimiter S, Kwong Peter D

Abstract excerpt

Antibodies m66.6 and 2F5 are the only effective human HIV-1-neutralizing antibodies reported thus far to recognize the N-terminal region of the membrane-proximal external region (MPER) of the gp41 subunit of the HIV-1 envelope glycoprotein. Although 2F5 has been extensively characterized, much less is known about antibody m66.6 or antibody m66, a closely related light-chain variant. Here, we report the crystal...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antibodies, Neutralizing
Share to Antigen-Antibody Complex

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Complementarity Determining Regions

Share to HIV Antibodies

Share to HIV Envelope Protein gp41

Share to Molecular Docking Simulation

Share to Neutralization Tests

Share to Protein Interaction Domains and Motifs

Source

Open in PubMed Open full text

Identifiers

PMID: 24335316
DOI: 10.1128/JVI.02837-13
PMCID: PMC3958054

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis for HIV-1 neutralization by 2F5-like antibodies m66 and m66.6.PMID 24335316Read ↗

Structural Analysis of the Epitope of the Anti-HIV Antibody 2F5 Sheds Light into Its Mechanism of Neutralization and HIV FusionSemantic proximity Read ↗

Structure and Mechanistic Analysis of the Anti-Human Immunodeficiency Virus Type 1 Antibody 2F5 in Complex with Its gp41 EpitopeSemantic proximity Read ↗

Crystallographic definition of the epitope promiscuity of the broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2F5: vaccine design implications.Semantic proximity Read ↗

Crystal Structure of Human Antibody 2909 Reveals Conserved Features of Quaternary Structure-Specific Antibodies That Potently Neutralize HIV-1Semantic proximity Read ↗

A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodiesSemantic proximity Read ↗

Crystal Structure of PG16 and Chimeric Dissection with Somatically Related PG9: Structure-Function Analysis of Two Quaternary-Specific Antibodies That Effectively Neutralize HIV-1Semantic proximity Read ↗

A multidonor class of highly glycan-dependent HIV-1 gp120-gp41 interface-targeting broadly neutralizing antibodiesSemantic proximity Read ↗

Role of HIV membrane in neutralization by two broadly neutralizing antibodies.Semantic proximity Read ↗

A human monoclonal antibody neutralizes diverse HIV-1 isolates by binding a critical gp41 epitopeSemantic proximity Read ↗

Neutralizing Antibodies Targeting HIV-1 gp41.Semantic proximity Read ↗

Dependence on a variable residue limits the breadth of an HIV MPER neutralizing antibody, despite convergent evolution with broadly neutralizing antibodiesSemantic proximity Read ↗

Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.