Conformational analysis in solution of gastrin releasing peptide
| Autor: | Joong-Hoon Ahn, K. Hun Mok, Yoongho Lim, Jin Hee Han, Choonshik Shin |
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| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular Protein Conformation Molecular Sequence Data Biophysics Peptide Bombina bombina Biochemistry chemistry.chemical_compound Gastrin-releasing peptide Gastrin-releasing peptide receptor Animals Amino Acid Sequence Receptor Nuclear Magnetic Resonance Biomolecular Molecular Biology Binding selectivity chemistry.chemical_classification biology Bombesin Cell Biology biology.organism_classification Solutions Gastrin-Releasing Peptide chemistry Bombesin-like peptides hormones hormone substitutes and hormone antagonists |
| Zdroj: | Biochemical and Biophysical Research Communications. 350:120-124 |
| ISSN: | 0006-291X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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