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Crystal structure of human bone morphogenetic protein-2 at 2.7 A resolution.

Abstract：

:Homodimeric bone morphogenetic protein-2 (BMP-2) is a member of the transforming growth factor beta (TGF-beta) superfamily that induces bone formation and regeneration, and determines important steps during early stages of embryonic development in vertebrates and non-vertebrates. BMP-2 can interact with two types of receptor chains, as well as with proteins of the extracellular matrix and several regulatory proteins. We report here the crystal structure of human BMP-2 determined by molecular replacement and refined to an R-value of 24.2 % at 2.7 A resolution. A common scaffold of BMP-2, BMP-7 and the TGF-betas, i.e. the cystine-knot motif and two finger-like double-stranded beta-sheets, can be superimposed with r. m.s. deviations of around 1 A. In contrast to the TGF-betas, the structure of BMP-2 shows differences in the flexibility of the N terminus and the orientation of the central alpha-helix as well as two external loops at the fingertips with respect to the scaffold. This is also known from the BMP-7 model. Small secondary structure elements in the loop regions of BMP-2 and BMP-7 seem to be specific for the respective BMP-subgroup. Two identical helix-finger clefts and two distinct cavities located around the central 2-fold axis of the dimer show characteristic shapes, polarity and surface charges. The possible function of these specific features in the interaction of BMP-2 with its binding partners is discussed.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Scheufler C,Sebald W,Hülsmeyer M

doi

10.1006/jmbi.1999.2590

keywords:

subject

Has Abstract

pub_date

1999-03-19 00:00:00

pages

103-15

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(99)92590-1

journal_volume

287

pub_type

杂志文章

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