Contrasting IgG Structures Reveal Extreme Asymmetry and Flexibility
- 24 May 2002
- journal article
- research article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 319 (1), 9-18
- https://doi.org/10.1016/s0022-2836(02)00244-9
Abstract
No abstract availableKeywords
This publication has 52 references indexed in Scilit:
- Molecular modelling study of HIV p17gag (MA) protein shell utilising data from electron microscopy and X-ray crystallographyJournal of Molecular Biology, 2000
- Crystallographic structure of an intact IgG1 monoclonal antibodyJournal of Molecular Biology, 1998
- Structural classification of CDR‐H3 in antibodiesFEBS Letters, 1996
- Structural Families in Loops of Homologous Proteins: Automatic Classification, Modelling and Application to AntibodiesJournal of Molecular Biology, 1996
- Direct Observation of Protein Solvation and Discrete Disorder with Experimental Crystallographic PhasesScience, 1996
- Molecular Profile of an Antibody Response to HIV-1 as Probed by Combinatorial LibrariesJournal of Molecular Biology, 1993
- X-ray Structures of the Antigen-binding Domains from Three Variants of Humanized anti-p185HER2 Antibody 4D5 and Comparison with Molecular ModelingJournal of Molecular Biology, 1993
- Characterization of crystals of an intact monoclonal antibody for canine lymphomaJournal of Molecular Biology, 1991
- Structure of the human antibody molecule kol (immunoglobulin G1): An electron density map at 5 Å resolutionJournal of Molecular Biology, 1976
- Electron microscopy of an antibody-hapten complexJournal of Molecular Biology, 1967