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Publication Abstract from PubMed

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.

Solution structure of betacellulin, a new member of EGF-family ligands.,Miura K, Doura H, Aizawa T, Tada H, Seno M, Yamada H, Kawano K Biochem Biophys Res Commun. 2002 Jun 28;294(5):1040-6. PMID:12074582^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.