2K3G

NMR structure analysis of a BMP receptor

2K3G の概要

• エントリーDOI: 10.2210/pdb2k3g/pdb
• NMR情報: BMRB: 15956
• 分子名称: Bone morphogenetic protein receptor type-1A (1 entity in total)
• 機能のキーワード: bmp, receptor, tgf-beta superfamily, atp-binding, disease mutation, glycoprotein, kinase, magnesium, manganese, membrane, metal-binding, nucleotide-binding, phosphoprotein, polymorphism, serine/threonine-protein kinase, transferase, transmembrane, signaling protein
• 由来する生物種: Homo sapiens
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P36894
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11278.69

構造登録者

Klages, J.,Kotzsch, A.,Mueller, T.,Kessler, H. (登録日: 2008-05-07, 公開日: 2008-12-16, 最終更新日: 2024-10-30)

主引用文献

Klages, J.,Kotzsch, A.,Coles, M.,Sebald, W.,Nickel, J.,Muller, T.,Kessler, H.
The solution structure of BMPR-IA reveals a local disorder-to-order transition upon BMP-2 binding.
Biochemistry, 47:11930-11939, 2008

PubMed Abstract: The structure of the extracellular domain of BMP receptor IA was determined in solution by NMR spectroscopy and compared to its structure when bound to its ligand BMP-2. While most parts of the secondary structure are highly conserved between the bound and unbound forms, large conformational rearrangements can be observed in the beta4beta5 loop of BMPR-IA, which is in contact with BMP-2 and harbors the main binding determinants for the BMPR-IA-BMP-2 interaction. In its unbound form, helix alpha1 in BMPR-IA, which is in the center of the binding epitope for BMP-2, is missing. Since BMP-2 also shows conformational changes in the type I receptor epitope upon binding to BMPR-IA, both binding partners pass through an induced fit mechanism to adapt their binding interfaces to a given interaction surface. The inherent flexibility of both partners possibly explains the promiscuous ligand-receptor interaction observed in the BMP protein superfamily.

PubMed: 18937504
DOI: 10.1021/bi801059j

実験手法

SOLUTION NMR