Conformational analysis in solution of gastrin releasing peptide

• Published in: Biochemical and biophysical research communications Vol. 350; no. 1; pp. 120 - 124
• Main Authors: Shin, Choonshik, Hun Mok, K., Han, Jin Hee, Ahn, Joong-Hoon, Lim, Yoongho
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 10.11.2006
• Subjects: Amino Acid Sequence; Animals; Bombesin-like peptides; Gastrin releasing peptide; Gastrin releasing peptide receptor; Gastrin-Releasing Peptide - chemistry; Models, Molecular; Molecular Sequence Data; NMR; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Solutions - chemistry; Three-dimensional structure; Gastrin releasing peptide; NMR; Gastrin releasing peptide receptor; Bombesin-like peptides; Three-dimensional structure
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2006.09.022

Gastrin releasing peptide (GRP) is the first peptide isolated from porcine gastric and intestinal tissues and is homologous to the carboxyl terminus of bombesin (Bn) isolated from the skin of the frog Bombina bombina. It is a member of the Bn-like peptides, which are important in numerous biological and pathological processes. The Bn-like peptides show high sequence homology in their C-terminal regions, but they have different selectivity for their receptors. In particular, GRP selectively binds to the GRP receptor (GRPR). However, the molecular basis for this selectivity remains largely unknown. Here, we report the three-dimensional structure of GRP. Hopefully, it could be helpful in a better understanding of the binding selectivity between GRP and GRPR.