Primary structure and conformational analysis of peptide methionine-tyrosine, a peptide related to neuropeptide Y and peptide YY isolated from lamprey intestine

TY - JOUR

T1 - Primary structure and conformational analysis of peptide methionine-tyrosine, a peptide related to neuropeptide Y and peptide YY isolated from lamprey intestine

AU - Conlon, J M

AU - Bjørnholm, B

AU - Jørgensen, Flemming Steen

AU - Youson, J H

AU - Schwartz, T W

PY - 1991

Y1 - 1991

N2 - 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-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 alpha-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 beta-turn between the two helical domains (residues 9-14) is appreciably different.

AB - 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-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 alpha-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 beta-turn between the two helical domains (residues 9-14) is appreciably different.

KW - Amino Acid Sequence

KW - Animals

KW - Chromatography, Gel

KW - Gastrointestinal Hormones

KW - Intestine, Small

KW - Lampreys

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Neuropeptide Y

KW - Peptide YY

KW - Peptides

KW - Protein Conformation

KW - Sequence Homology, Nucleic Acid

U2 - 10.1111/j.1432-1033.1991.tb16123.x

DO - 10.1111/j.1432-1033.1991.tb16123.x

M3 - Journal article

C2 - 2070789

SN - 1742-464X

VL - 199

SP - 293

EP - 298

JO - FEBS Journal

JF - FEBS Journal

IS - 2

ER -