2MBK

The Clip-segment of the von Willebrand domain 1 of the BMP modulator protein Crossveinless 2 is preformed

2MBK の概要

• エントリーDOI: 10.2210/pdb2mbk/pdb
• NMR情報: BMRB: 19403
• 分子名称: Crossveinless 2 (1 entity in total)
• 機能のキーワード: von willebrand type c domain, bmp modulator, crossveinless 2, bmper, signaling protein
• 由来する生物種: Danio rerio (zebra fish)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7336.42

構造登録者

Mueller, T.D.,Fiebig, J.E.,Weidauer, S.E.,Qiu, L.,Bauer, M.,Schmieder, P.,Beerbaum, M.,Zhang, J.,Oschkinat, H.,Sebald, W. (登録日: 2013-08-02, 公開日: 2013-10-16, 最終更新日: 2024-10-30)

主引用文献

Fiebig, J.E.,Weidauer, S.E.,Qiu, L.Y.,Bauer, M.,Schmieder, P.,Beerbaum, M.,Zhang, J.L.,Oschkinat, H.,Sebald, W.,Mueller, T.D.
The Clip-Segment of the von Willebrand Domain 1 of the BMP Modulator Protein Crossveinless 2 Is Preformed.
Molecules, 18:11658-11682, 2013

PubMed Abstract: Bone Morphogenetic Proteins (BMPs) are secreted protein hormones that act as morphogens and exert essential roles during embryonic development of tissues and organs. Signaling by BMPs occurs via hetero-oligomerization of two types of serine/threonine kinase transmembrane receptors. Due to the small number of available receptors for a large number of BMP ligands ligand-receptor promiscuity presents an evident problem requiring additional regulatory mechanisms for ligand-specific signaling. Such additional regulation is achieved through a plethora of extracellular antagonists, among them members of the Chordin superfamily, that modulate BMP signaling activity by binding. The key-element in Chordin-related antagonists for interacting with BMPs is the von Willebrand type C (VWC) module, which is a small domain of about 50 to 60 residues occurring in many different proteins. Although a structure of the VWC domain of the Chordin-member Crossveinless 2 (CV2) bound to BMP-2 has been determined by X-ray crystallography, the molecular mechanism by which the VWC domain binds BMPs has remained unclear. Here we present the NMR structure of the Danio rerio CV2 VWC1 domain in its unbound state showing that the key features for high affinity binding to BMP-2 is a pre-oriented peptide loop.

PubMed: 24071977
DOI: 10.3390/molecules181011658

実験手法

SOLUTION NMR