Helmholtz Gemeinschaft

Search
Browse
Statistics
Feeds

A complex water network contributes to high-affinity binding in an antibody-antigen interface

[img] PDF (Article) - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
1MB
[img] PDF (Supplementary material) - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
1MB

Item Type:Article
Title:A complex water network contributes to high-affinity binding in an antibody-antigen interface
Creators Name:Marino, S.F. and Olal, D. and Daumke, O.
Abstract:This data article presents an analysis of structural water molecules in the high affinity interaction between a potent tumor growth inhibiting antibody (fragment), J22.9-xi, and the tumor marker antigen CD269 (B cell maturation antigen, BCMA). The 1.89 {Angstrom} X-ray crystal structure shows exquisite details of the binding interface between the two molecules, which comprises relatively few, mostly hydrophobic, direct contacts but many indirect interactions over solvent waters. These are partly or wholly buried in, and therefore part of, the interface. A partial description of the structure is included in an article on the tumor inhibiting effects of the antibody: "Potent anti-tumor response by targeting B cell maturation antigen (BCMA) in a mouse model of multiple myeloma", Mol. Oncol. 9 (7) (2015) pp. 1348–58.
Keywords:Crystal Structure, Fab Fragment, BCMA, Binding Interface, High Affinity, Water Molecules, Animals, Mice
Source:Data in Brief
ISSN:2352-3409
Publisher:Elsevier (The Netherlands)
Volume:6
Page Range:394-397
Date:March 2016
Official Publication:https://doi.org/10.1016/j.dib.2015.12.023
PubMed:View item in PubMed

Repository Staff Only: item control page

Downloads

Downloads per month over past year

Open Access
MDC Library