Pancreatic hormone

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Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Pancreatic hormone peptide
Identifiers
Symbol	Hormone_3
Pfam	PF00159
InterPro	IPR001955
PROSITE	PDOC00238
SCOP	1ppt
SUPERFAMILY	1ppt
OPM protein	1icy
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]

Pancreatic hormones (PP)^[1] are peptides synthesized in pancreatic islets of Langherhans, 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^[2] and has an amidated C terminus^[3]. 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^[2]. Unlike glucagon, another peptide hormone, the structure of pancreatic peptide is preserved in aqueous solution^[4]. Both N and C termini are required for activity: receptor binding and activation functions may reside in the N and C termini respectively^[2].

Subfamilies[edit | edit source]

Pancreatic hormone subtype InterPro: IPR015480
Peptide YY InterPro: IPR015481

Human proteins containing this domain[edit | edit source]

NPY; PPY; PYY;

References[edit | edit source]

↑ Humbel RE, Blundell TL (1980). "Hormone families: pancreatic hormones and homologous growth factors". Nature. 287 (5785): 781–787. doi:10.1038/287781a0. PMID 6107857. line feed character in |title= at position 18 (help)
↑ ^2.0 ^2.1 ^2.2 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. PMID 3031687.
↑ 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.
↑ 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

Template:WH Template:WS

[PUB00003973-1] Humbel RE, Blundell TL (1980). "Hormone families: pancreatic hormones and homologous growth factors". Nature. 287 (5785): 781–787. doi:10.1038/287781a0. PMID 6107857. line feed character in |title= at position 18 (help)

[PUB00004634-2] 2.0 ^2.1 ^2.2 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. PMID 3031687.

[PUB00001581-3] 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.

[PUB00004503-4] 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.

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