Conformational analysis in solution of gastrin releasing peptide.
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.
Shin
Choonshik
C
Bio/Molecular Informatics Center, Division of Bioscience and Biotechnology, IBST, Konkuk University, Seoul 143-701, Republic of Korea.
Mok
K Hun
KH
Han
Jin Hee
JH
Ahn
Joong-Hoon
JH
Lim
Yoongho
Y
D000595:Amino Acid Sequence; D000818:Animals; D019886:Gastrin-Releasing Peptide / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D012996:Solutions / Q000737:chemistry
D012996:Solutions; D019886:Gastrin-Releasing Peptide