Pancreatic hormone

Pancreatic hormone peptide
Structure of avian pancreatic polypeptide.[1]
Identifiers
Symbol Hormone_3
Pfam PF00159
InterPro IPR001955
PROSITE PDOC00238
SCOP 1ppt
OPM protein 1icy

Pancreatic hormones (PP)[2] are peptides synthesized in pancreatic islets of Langerhans, which acts as a regulator of pancreatic and gastrointestinal functions.

The hormone is produced as a larger propeptide, which is enzymatically cleaved to yield the mature active peptide: this is 36 amino acids in length[3] and has an amidated C terminus.[4] The hormone has a globular structure, residues 2-8 forming a left-handed poly-proline-II-like helix, residues 9-13 a beta turn, and 14-32 an alpha-helix,held close to the first helix by hydrophobic interactions.[3] Unlike glucagon, another peptide hormone, the structure of pancreatic peptide is preserved in aqueous solution.[5] Both N and C termini are required for activity: receptor binding and activation functions may reside in the N and C termini respectively.[3]

Subfamilies

Human proteins containing this domain

NPY; PPY; PYY;

References

  1. ^ Blundell TL, Pitts JE, Tickle IJ, Wood SP, Wu CW (July 1981). "X-ray analysis (1. 4-A resolution) of avian pancreatic polypeptide: Small globular protein hormone". Proc. Natl. Acad. Sci. U.S.A. 78 (7): 4175–4179. doi:10.1073/pnas.78.7.4175. PMC 319751. PMID 16593056. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=319751. 
  2. ^ Humbel RE, Blundell TL (1980). "Hormone families: pancreatic hormones and homologous growth factors". Nature 287 (5785): 781–787. doi:10.1038/287781a0. PMID 6107857. 
  3. ^ a b c Martin J, Allen J, Novotny J, Heinrich G (1987). "Molecular structure of mammalian neuropeptide Y: analysis by molecular cloning and computer-aided comparison with crystal structure of avian homologue". Proc. Natl. Acad. Sci. U.S.A. 84 (8): 2532–2536. doi:10.1073/pnas.84.8.2532. PMC 304688. PMID 3031687. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=304688. 
  4. ^ Mutt V, Sillard R, Agerberth B, Jornvall H (1989). "Sheep neuropeptide Y. A third structural type of a highly conserved peptide". FEBS Lett. 258 (2): 263–265. doi:10.1016/0014-5793(89)81669-2. PMID 2599092. 
  5. ^ Conlon JM, Thim L, Bjenning C, Moon TW, Youson JH (1991). "Neuropeptide Y-related peptides from the pancreas of a teleostean (eel), holostean (bowfin) and elasmobranch (skate) fish". Peptides 12 (2): 221–226. doi:10.1016/0196-9781(91)90003-8. PMID 2067973. 

This article incorporates text from the public domain Pfam and InterPro IPR001955