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

ABSTRACT: 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.

SUBMITTER: Harth S

PROVIDER: S-EPMC2917305 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature

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

Harth Stefan S Kotzsch Alexander A Sebald Walter W Mueller Thomas Dieter TD

Acta crystallographica. Section F, Structural biology and crystallization communications 20100729 Pt 8

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 ...[more]

PMID: 20693682

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