Published July 29, 2010 | Version v1
Journal article

Crystallization of BMP receptor type IA bound to the antibody Fab fragment AbD1556

  • 1. Lehrstuhl für Physiologische Chemie II, Biozentrum der Universität Würzburg, Am Hubland, D-97074 Würzburg (Germany)
  • 2. Lehrstuhl für Molekulare Pflanzenphysiologie und Biophysik, Julius-von-Sachs Institut der Universität Würzburg, Julius-von-Sachs Platz 2, D-97082 Würzburg (Germany)

Description

The crystallization of BMP receptor type IA bound to the neutralizing antibody Fab fragment AbD1556 obtained by phage-display selection is reported. An antibody Fab fragment, AbD1556, was selected against the extracellular domain of BMP receptor type IA, which blocks the binding of BMP-2 to BMPR-IA and thereby neutralizes BMP-2 activity. To study the mechanism by which BMPR-IA is recognized and bound by the Fab fragment, the complex of AbD1556 bound to BMPR-IA was prepared and crystallized. Crystals of this binary complex belonged to the monoclinic space group P21, with unit-cell parameters a = 89.32, b = 129.25, c = 100.24 Å, β = 92.27°

Availability note (English)

Available from http://dx.doi.org/10.1107/S1744309110024681; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2917305

Additional details

Publishing Information

Journal Title
Acta Crystallographica. Section F
Journal Volume
66
Journal Issue
Pt 8
Journal Page Range
p. 964-968
ISSN
1744-3091
CODEN
ACSFCL

INIS

Country of Publication
United Kingdom
Country of Input or Organization
International Atomic Energy Agency (IAEA)
INIS RN
46072637
Subject category
S75: CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY;
Descriptors DEI
CRYSTALLIZATION; CRYSTALS; RECEPTORS; SPACE GROUPS
Descriptors DEC
MEMBRANE PROTEINS; ORGANIC COMPOUNDS; PHASE TRANSFORMATIONS; PROTEINS; SYMMETRY GROUPS

Optional Information

Copyright
Copyright (c) International Union of Crystallography 2010
Notes
PMCID: PMC2917305; PMID: 20693682; PUBLISHER-ID: fw5265; OAI: oai:pubmedcentral.nih.gov:2917305