Crystal Structure of a Bivalent Antibody Fab Fragment.
Amino Acid Sequence
Amino Acid Substitution
Antibodies, Bispecific
/ chemistry
Antibody Affinity
Cryoelectron Microscopy
Crystallography, X-Ray
Immunoglobulin Fab Fragments
/ chemistry
Models, Molecular
Mutation
Protein Conformation
Protein Multimerization
Recombinant Proteins
Spectrum Analysis
Structure-Activity Relationship
Thermodynamics
antibody
domain swapping
fab
structure
Journal
Journal of molecular biology
ISSN: 1089-8638
Titre abrégé: J Mol Biol
Pays: Netherlands
ID NLM: 2985088R
Informations de publication
Date de publication:
22 01 2021
22 01 2021
Historique:
received:
19
08
2020
revised:
29
10
2020
accepted:
11
11
2020
pubmed:
22
11
2020
medline:
27
4
2021
entrez:
21
11
2020
Statut:
ppublish
Résumé
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 V
Identifiants
pubmed: 33220264
pii: S0022-2836(20)30632-X
doi: 10.1016/j.jmb.2020.11.013
pii:
doi:
Substances chimiques
Antibodies, Bispecific
0
Immunoglobulin Fab Fragments
0
Recombinant Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
166714Informations de copyright
Copyright © 2020 Elsevier Ltd. All rights reserved.