3BMP

HUMAN BONE MORPHOGENETIC PROTEIN-2 (BMP-2)

「2BMP」から置き換えられました

3BMP の概要

• エントリーDOI: 10.2210/pdb3bmp/pdb
• 分子名称: PROTEIN (BONE MORPHOGENETIC PROTEIN 2 (BMP-2)), (4S)-2-METHYL-2,4-PENTANEDIOL (3 entities in total)
• 機能のキーワード: cytokine, bone morphogenetic protein, cystin-knot, tgfb-family
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P12643
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13042.03

構造登録者

Scheufler, C.,Sebald, W.,Huelsmeyer, M. (登録日: 1999-03-12, 公開日: 2000-03-12, 最終更新日: 2024-11-13)

主引用文献

Scheufler, C.,Sebald, W.,Hulsmeyer, M.
Crystal structure of human bone morphogenetic protein-2 at 2.7 A resolution.
J.Mol.Biol., 287:103-115, 1999

PubMed 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.

PubMed: 10074410
DOI: 10.1006/jmbi.1999.2590

実験手法

X-RAY DIFFRACTION (2.7 Å)