PDBsum entry 2mbk

Signaling protein

PDB id: 2mbk

Contents

Protein chain

67 a.a.

PDB id:

2mbk

Name:

Signaling protein

Title:

The clip-segment of the von willebrand domain 1 of the bmp modulator protein crossveinless 2 is preformed

Structure:

Crossveinless 2. Chain: a. Fragment: unp residues 28-93. Engineered: yes

Source:

Danio rerio. Zebra fish. Organism_taxid: 7955. Gene: bmper, cvl2, id:ibd5071. Expressed in: escherichia coli. Expression_system_taxid: 469008.

NMR struc:

10 models

Authors:

T.D.Mueller,J.E.Fiebig,S.E.Weidauer,L.Qiu,M.Bauer,P.Schmieder, M.Beerbaum,J.Zhang,H.Oschkinat,W.Sebald

Key ref:

J.E.Fiebig et al. (2013). The clip-segment of the von Willebrand domain 1 of the BMP modulator protein Crossveinless 2 is preformed. Molecules, 18, 11658-11682. PubMed id: 24071977 DOI: 10.3390/molecules181011658

Date:

02-Aug-13 Release date: 16-Oct-13

Protein chain

Q5D734  (Q5D734_DANRE) -  Crossveinless 2 from Danio rerio

Seq: 668 a.a.

Struc: 67 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.3390/molecules181011658

Molecules 18:11658-11682 (2013)

PubMed id: 24071977

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

J.E.Fiebig, S.E.Weidauer, L.Y.Qiu, M.Bauer, P.Schmieder, M.Beerbaum, J.L.Zhang, H.Oschkinat, W.Sebald, T.D.Mueller.

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.