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

Crystal Structure of a Bivalent Antibody Fab Fragment.

Journal of molecular biology - 22 Jan 2021

Shahid Salman, Gao Mingming, Travis Gallagher D, Pozharski Edwin, Brinson Robert G, Keck Zhen-Yong, Foung Steven K H, Fuerst Thomas R, Mariuzza Roy A

Abstract excerpt

We determined the crystal structure to 1.8 Å resolution of the Fab fragment of an affinity-matured human monoclonal antibody (HC84.26.5D) that recognizes the E2 envelope glycoprotein of hepatitis C virus (HCV). Unlike conventional Fabs, which are monovalent monomers, Fab HC84.26.5D assembles into a bivalent domain-swapped dimer in which the two VL/VH modules are separated by ~25 Å. In solution, Fab HC84.26.5D...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies, Bispecific
Share to Antibody Affinity

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cryoelectron Microscopy

Share to Crystallography, X-Ray

Share to Immunoglobulin Fab Fragments

Share to Protein Multimerization

Share to Spectrum Analysis

Share to Thermodynamics

Source

Identifiers

PMID: 33220264
DOI: 10.1016/j.jmb.2020.11.013

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

Crystal Structure of a Bivalent Antibody Fab Fragment.PMID 33220264Read ↗

Structure of the hepatitis C virus E1E2 glycoprotein complexSemantic proximity Read ↗

Structure of engineered hepatitis C virus E1E2 ectodomain in complex with neutralizing antibodiesSemantic proximity Read ↗

A highly potent human antibody neutralizes dengue virus serotype 3 by binding across three surface proteins.Semantic proximity Read ↗

Antibody Domain Exchange Is an Immunological Solution to Carbohydrate Cluster RecognitionSemantic proximity Read ↗

IgG3 Hinge Architecture Expands Dengue Virus Breadth of A Quaternary Epitope Dependent Zika Virus Cross-Neutralizing AntibodySemantic proximity Read ↗

Affinity maturation of a portable Fab-RNA module for chaperone-assisted RNA crystallography.Semantic proximity Read ↗

Structure-guided affinity maturation of a single-chain variable fragment antibody against the Fu-bc epitope of the dengue virus envelope proteinSemantic proximity Read ↗

Structural flexibility at a major conserved antibody target on hepatitis C virus E2 antigenSemantic proximity Read ↗

Structure of a Neutralizing Antibody Bound Monovalently to Human Rhinovirus 2Semantic proximity Read ↗

Next generation Fc scaffold for multispecific antibodiesSemantic proximity Read ↗

Broadly neutralizing anti-hepatitis B virus antibody reveals a complementarity determining region H3 lid-opening mechanism.Semantic proximity Read ↗

Combining computational modeling and experimental library screening to affinity-mature VEEV-neutralizing antibody F5Semantic proximity Read ↗

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