| Literature DB >> 24668560 |
Juan C Almagro1, Alexey Teplyakov, Jinquan Luo, Raymond W Sweet, Sreekumar Kodangattil, Francisco Hernandez-Guzman, Gary L Gilliland.
Abstract
To assess the state of the art in antibody 3D modeling, 11 unpublished high-resolution x-ray Fab crystal structures from diverse species and covering a wide range of antigen-binding site conformations were used as a benchmark to compare Fv models generated by seven structure prediction methodologies. The participants included: Accerlys Inc, Chemical Computer Group (CCG), Schrodinger, Jeff Gray's lab at John Hopkins University, Macromoltek, Astellas Pharma/Osaka University and Prediction of ImmunoGlobulin Structure (PIGS). The sequences of benchmark structures were submitted to the modelers and PIGS, and a set of models were generated for each structure. We provide here an overview of the organization, participants and main results of this second antibody modeling assessment (AMA-II). Also, we compare the results with the first antibody assessment published in this journal (Almagro et al., 2011;79:3050).Entities:
Keywords: antigen-binding site; canonical structures; homology modeling; immunoglobulin; x-ray structure
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Year: 2014 PMID: 24668560 DOI: 10.1002/prot.24567
Source DB: PubMed Journal: Proteins ISSN: 0887-3585