Primary structure and conformational analysis of peptide methionine-tyrosine, a peptide related to neuropeptide Y and peptide YY isolated from lamprey intestine
Autor: | J H Youson, B Bjørnholm, Flemming Jørgensen, J M Conlon, Thue W. Schwartz |
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Rok vydání: | 1991 |
Předmět: |
Models
Molecular Protein Conformation Molecular Sequence Data Peptide Biology Biochemistry Gastrointestinal Hormones chemistry.chemical_compound Protein structure Sequence Homology Nucleic Acid Intestine Small Animals Neuropeptide Y Peptide YY Amino Acid Sequence Tyrosine Peptide sequence chemistry.chemical_classification Methionine Protein primary structure Lampreys Neuropeptide Y receptor chemistry Chromatography Gel Peptides |
Zdroj: | European Journal of Biochemistry. 199:293-298 |
ISSN: | 1432-1033 0014-2956 |
DOI: | 10.1111/j.1432-1033.1991.tb16123.x |
Popis: | A peptide belonging to the pancreatic-polypeptide-fold family of regulatory peptides has been isolated from the intestine of an Agnathan, the sea lamprey (Petromyzon marinus). The primary structure of the peptide (termed peptide methionine – tyrosine) was established as Met-Pro-Pro-Lys-Pro-Asp-Asn-Pro-Ser-Pro10-Asp-Ala-Ser-Pro-Glu-Glu-Leu-Ser-Lys-Tyr20-Met-Leu-Ala-Val-Arg-Asn-Tyr-Ile-Asn-Leu30-Ile-Thr-Arg-Gln-Arg-Tyr CONH2. This sequence shows stronger structural similarity with pig neuropeptide Y (64%), particularly in the COOH-terminal region, than with pig peptide tyrosine – tyrosine (61%) or with pig pancreatic polypeptide (42%). Molecular modelling and dynamic simulation, based upon sequence similarity with turkey pancreatic polypeptide, indicates that the conformations of the polyproline-helix-like region (residues 1–8) and the α-helical region (residues 15–30) in turkey pancreatic polypeptide are conserved in peptide methionine – tyrosine, and that non-bonded interactions between these domains have preserved the overall polypeptide fold in the molecule. The substitution of the otherwise totally conserved Gly9 residue by serine in lamprey peptide methionine – tyrosine, however, results in a preferred structure in which the conformation of the β-turn between the two helical domains (residues 9–14) is appreciably different. |
Databáze: | OpenAIRE |
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