2MBK
The Clip-segment of the von Willebrand domain 1 of the BMP modulator protein Crossveinless 2 is preformed
Summary for 2MBK
| Entry DOI | 10.2210/pdb2mbk/pdb |
| NMR Information | BMRB: 19403 |
| Descriptor | Crossveinless 2 (1 entity in total) |
| Functional Keywords | von willebrand type c domain, bmp modulator, crossveinless 2, bmper, signaling protein |
| Biological source | Danio rerio (zebra fish) |
| Total number of polymer chains | 1 |
| Total formula weight | 7336.42 |
| Authors | Mueller, T.D.,Fiebig, J.E.,Weidauer, S.E.,Qiu, L.,Bauer, M.,Schmieder, P.,Beerbaum, M.,Zhang, J.,Oschkinat, H.,Sebald, W. (deposition date: 2013-08-02, release date: 2013-10-16, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 24071977DOI: 10.3390/molecules181011658 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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