PDBsum entry 2hlq

Transferase

PDB id: 2hlq

Contents

Protein chain

100 a.a. *

Waters ×92

* Residue conservation analysis

PDB id:

2hlq

Name:

Transferase

Title:

Crystal structure of the extracellular domain of the type ii bmp receptor

Structure:

Bone morphogenetic protein receptor type-2. Chain: a. Fragment: residues 32-131. Synonym: bone morphogenetic receptor type ii, bmprii. Engineered: yes

Source:

Ovis aries. Sheep. Organism_taxid: 9940. Gene: bmprii. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.45Å R-factor: 0.192 R-free: 0.232

Authors:

P.D.Mace,J.F.Cutfield,S.M.Cutfield

Key ref:

P.D.Mace et al. (2006). High resolution structures of the bone morphogenetic protein type II receptor in two crystal forms: implications for ligand binding. Biochem Biophys Res Commun, 351, 831-838. PubMed id: 17094948 DOI: 10.1016/j.bbrc.2006.10.109

Date:

09-Jul-06 Release date: 28-Nov-06

Protein chain

Q13873  (BMPR2_HUMAN) -  Bone morphogenetic protein receptor type-2 from Homo sapiens

Seq: 1038 a.a.

Struc: 100 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.2.7.11.30 - receptor protein serine/threonine kinase.
• Reaction:
  1. L-seryl-[receptor-protein] + ATP = O-phospho-L-seryl-[receptor- protein] + ADP + H⁺
  2. L-threonyl-[receptor-protein] + ATP = O-phospho-L-threonyl-[receptor- protein] + ADP + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.bbrc.2006.10.109

Biochem Biophys Res Commun 351:831-838 (2006)

PubMed id: 17094948

High resolution structures of the bone morphogenetic protein type II receptor in two crystal forms: implications for ligand binding.

P.D.Mace, J.F.Cutfield, S.M.Cutfield.

ABSTRACT

BMPRII is a type II TGF-beta serine threonine kinase receptor which is integral to the bone morphogenetic protein (BMP) signalling pathway. It is known to bind BMP and growth differentiation factor (GDF) ligands, and has overlapping ligand specificity with the activin type II receptor, ActRII. In contrast to activin and TGF-beta type ligands, BMPs bind to type II receptors with lower affinity than type I receptors. Crystals of the BMPRII ectodomain were grown in two different forms, both of which diffracted to high resolution. The tetragonal form exhibited some disorder, whereas the entire polypeptide was seen in the orthorhombic form. The two structures retain the basic three-finger toxin fold of other TGF-beta receptor ectodomains, and share the main hydrophobic patch used by ActRII to bind various ligands. However, they present different conformations of the A-loop at the periphery of the proposed ligand-binding interface, in conjunction with rearrangement of a disulfide bridge within the loop. This particular disulfide (Cys94-Cys117) is only present in BMPRII and activin receptors, suggesting that it is important for their likely shared mode of binding. Evidence is presented that the two crystal forms represent ligand-bound and free conformations of BMPRII. Comparison with the solved structure of ActRII bound to BMP2 suggests that His87, unique amongst TGF-beta receptors, may play a key role in ligand recognition.