Primary structure and conformational analysis of peptide methionine-tyrosine, a peptide related to neuropeptide Y and peptide YY isolated from lamprey intestine
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
Primary structure and conformational analysis of peptide methionine-tyrosine, a peptide related to neuropeptide Y and peptide YY isolated from lamprey intestine. / Conlon, J M; Bjørnholm, B; Jørgensen, Flemming Steen; Youson, J H; Schwartz, T W.
In: European Journal of Biochemistry, Vol. 199, No. 2, 1991, p. 293-8.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
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
VL - 199
SP - 293
EP - 298
JO - FEBS Journal
JF - FEBS Journal
SN - 1742-464X
IS - 2
ER -
ID: 38394633