1REW

Structural refinement of the complex of bone morphogenetic protein 2 and its type IA receptor

1REW の概要

• エントリーDOI: 10.2210/pdb1rew/pdb
• 関連するPDBエントリー: 1ES7 1REU 3BMP
• 分子名称: bone morphogenetic protein 2, bone morphogenetic protein receptor type IA (3 entities in total)
• 機能のキーワード: tgf-beta fold; bria-fold; 3-finger toxin fold, hormone-growth factor-signaling protein complex, hormone/growth factor/signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 55196.61

構造登録者

Keller, S.,Nickel, J.,Zhang, J.-L.,Sebald, W.,Mueller, T.D. (登録日: 2003-11-07, 公開日: 2004-05-04, 最終更新日: 2024-10-30)

主引用文献

Keller, S.,Nickel, J.,Zhang, J.L.,Sebald, W.,Mueller, T.D.
Molecular recognition of BMP-2 and BMP receptor IA.
Nat.Struct.Mol.Biol., 11:481-488, 2004

PubMed Abstract: Bone morphogenetic protein-2 (BMP-2) and other members of the TGF-beta superfamily regulate the development, maintenance and regeneration of tissues and organs. Binding epitopes for these extracellular signaling proteins have been defined, but hot spots specifying binding affinity and specificity have so far not been identified. In this study, mutational and structural analyses show that epitopes of BMP-2 and the BRIA receptor form a new type of protein-protein interface. The main chain atoms of Leu 51 and Asp53 of BMP-2 represent a hot spot of binding to BRIA. The BMP-2 variant L51P was deficient in type I receptor binding only, whereas its overall structure and its binding to type II receptors and modulator proteins, such as noggin, were unchanged. Thus, the L51P substitution converts BMP-2 into a receptor-inactive inhibitor of noggin. These results are relevant for other proteins of the TGF-beta superfamily and provide useful clues for structure-based drug design.

PubMed: 15064755
DOI: 10.1038/nsmb756

実験手法

X-RAY DIFFRACTION (1.863 Å)