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Crystallization of BMP receptor type IA bound to the antibody Fab fragment AbD1556
Stefan Harth1, Alexander Kotzsch, Walter Sebald
1Lehrstuhl für Physiologische Chemie II, Biozentrum der Universität Würzburg, Am Hubland, D-97074 Würzburg, Germany.
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 P2(1), with unit-cell parameters a=89.32, b=129.25, c=100.24 A, beta=92.27 degrees.
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 P2(1), with unit-cell parameters a=89.32, b=129.25, c=100.24 A, beta=92.27 degrees.
