1IP0

NMR STRUCTURE OF HUMAN BETACELLULIN-2

Summary for 1IP0

• Entry DOI: 10.2210/pdb1ip0/pdb
• Related: 1IOX
• Descriptor: BETACELLULIN (1 entity in total)
• Functional Keywords: egf-like fold, hormone-growth factor complex, hormone/growth factor
• Biological source: Homo sapiens (human)
• Cellular location: Betacellulin: Secreted, extracellular space. Probetacellulin: Cell membrane; Single-pass type I membrane protein: P35070
• Total number of polymer chains: 1
• Total formula weight: 5916.89

Authors

Miura, K.,Doura, H.,Aizawa, T.,Tada, H.,Seno, M.,Yamada, H.,Kawano, K. (deposition date: 2001-04-19, release date: 2002-07-31, Last modification date: 2024-11-20)

Primary citation

Miura, K.,Doura, H.,Aizawa, T.,Tada, H.,Seno, M.,Yamada, H.,Kawano, K.
Solution structure of betacellulin, a new member of EGF-family ligands.
Biochem.Biophys.Res.Commun., 294:1040-1046, 2002

PubMed 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.

PubMed: 12074582
DOI: 10.1016/S0006-291X(02)00585-5

Experimental method

SOLUTION NMR