PDBsum entry 1ip0

Hormone/growth factor

PDB id

1ip0

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Contents

			Protein chain

					50 a.a. *

* Residue conservation analysis

PDB id:

1ip0

Links
- PDBe
- RCSB
- MMDB
- JenaLib
- Proteopedia
- CATH
- SCOP
- PDBSWS
- ProSAT

Name:

Hormone/growth factor

Title:

Nmr structure of human betacellulin-2

Structure:

Betacellulin. Chain: a. Fragment: residues 62-111. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

1 models

Authors:

K.Miura,H.Doura,T.Aizawa,H.Tada,M.Seno,H.Yamada,K.Kawano

Key ref:

K.Miura et al. (2002). Solution structure of betacellulin, a new member of EGF-family ligands. Biochem Biophys Res Commun, 294, 1040-1046. PubMed id: 12074582 DOI: 10.1016/S0006-291X(02)00585-5

Date:

19-Apr-01

Release date:

31-Jul-02

PROCHECK

	Headers

	References

Protein chain

P35070 (BTC_HUMAN) - Probetacellulin from Homo sapiens

Seq: Struc:					178 a.a. 50 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

DOI no: 10.1016/S0006-291X(02)00585-5	Biochem Biophys Res Commun 294:1040-1046 (2002)
PubMed id: 12074582

Solution structure of betacellulin, a new member of EGF-family ligands.
K.Miura, H.Doura, T.Aizawa, H.Tada, M.Seno, H.Yamada, K.Kawano.

ABSTRACT

The solution structure of the EGF-like domain of betacellulin (BTCe), a newly discovered member of the epidermal growth factor (EGF) family, has been determined using two-dimensional nuclear magnetic resonance spectroscopy. This is the first report to identify the solution structure of the EGF-family ligand monomers that interact with both ErbB-1 and ErbB-4. The solution structure of BTCe was calculated using 538 NMR-derived restraints. The overall structure of BTCe was stabilized by three disulfide bonds, a hydrophobic core, and 23 hydrogen bonds. It appears that BTCe is comprised of five beta-strands and one short 3(10) helical turn. The secondary structural elements of BTCe are basically similar to those of the other EGF-family proteins, except that several significant variations of the structural properties were found. It is suggested that the structural variations between BTCe and the other EGF-family ligands may affect the specific receptor-recognition properties of EGF-family ligands.

Literature references that cite this PDB file's key reference

PubMed id

Reference

12869572

M.Wingens, T.Walma, H.van Ingen, C.Stortelers, J.E.van Leeuwen, E.J.van Zoelen, and G.W.Vuister (2003).
Structural analysis of an epidermal growth factor/transforming growth factor-alpha chimera with unique ErbB binding specificity.

J Biol Chem, 278, 39114-39123.

PDB code:

1p9j

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.