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

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 b...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2010-08, Vol.66 (8), p.964-968
Main Authors: Harth, Stefan, Kotzsch, Alexander, Sebald, Walter, Mueller, Thomas Dieter
Format: Article
Language:English
Subjects:
antibody Fab fragments
Antigen-Antibody Complex - chemistry
Antigen-Antibody Complex - immunology
Bone Morphogenetic Protein Receptors, Type I - chemistry
Bone Morphogenetic Protein Receptors, Type I - immunology
bone morphogenetic proteins
Crystallization
Crystallization Communications
Crystallography, X-Ray
Crystals
Humans
Immunoglobulin Fab Fragments - chemistry
Immunoglobulin Fab Fragments - immunology
protein-protein recognition
TGF-β superfamily
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Summary: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°.
ISSN:1744-3091
1744-3091
2053-230X
DOI:10.1107/S1744309110024681