1ppt

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[[Image:1ppt.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ppt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ppt OCA], [http://www.ebi.ac.uk/pdbsum/1ppt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ppt RCSB]</span>
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'''X-RAY ANALYSIS (1.4-ANGSTROMS RESOLUTION) OF AVIAN PANCREATIC POLYPEPTIDE. SMALL GLOBULAR PROTEIN HORMONE'''
'''X-RAY ANALYSIS (1.4-ANGSTROMS RESOLUTION) OF AVIAN PANCREATIC POLYPEPTIDE. SMALL GLOBULAR PROTEIN HORMONE'''
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[[Category: Tickle, I J.]]
[[Category: Tickle, I J.]]
[[Category: Wood, S P.]]
[[Category: Wood, S P.]]
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[[Category: pancreatic hormone]]
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[[Category: Pancreatic hormone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:20:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:02:54 2008''
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Revision as of 02:20, 3 May 2008

Template:STRUCTURE 1ppt

X-RAY ANALYSIS (1.4-ANGSTROMS RESOLUTION) OF AVIAN PANCREATIC POLYPEPTIDE. SMALL GLOBULAR PROTEIN HORMONE


Overview

The crystal structure of avian pancreatic polypeptide (aPP), a 36-residue polypeptide with some hormonal properties, has been determined by using single isomorphous replacement and anomalous scattering to 2.1-A resolution. The phases were extended to 1.4-A resolution by using a modified tangent formula. The molecule contains two regions of secondary structure-an extended polyproline-like helix (residues 1-8) and an alpha-helix (residues 14-31)-that run roughly antiparallel. The packing together of nonpolar groups from these regions gives the molecule a hydrophobic core in spite of its small size. The aPP molecules form a symmetrical dimer in the crystal stabilized principally by interlocking of nonpolar groups from the alpha-helices. The aPP dimers are crosslinked by coordination of Zn(2+); three aPP molecules contribute ligands to each zinc. The coordination geometry is a distorted trigonal bipyramid. The properties of the aPP molecule in solution are consistent with expectations based on the crystal structure. The aPP molecule has several general features in common with the pancreatic hormones insulin and glucagon. All three hormones have complex mechanisms for self-association. Like insulin, aPP seems to have a stable monomeric structure but its biological activity seems to depend on the more flexible COOH-terminal region analogous to the flexible NH(2)-terminal region of glucagon.

About this Structure

1PPT is a Single protein structure of sequence from Meleagris gallopavo. Full crystallographic information is available from OCA.

Reference

X-ray analysis (1. 4-A resolution) of avian pancreatic polypeptide: Small globular protein hormone., Blundell TL, Pitts JE, Tickle IJ, Wood SP, Wu CW, Proc Natl Acad Sci U S A. 1981 Jul;78(7):4175-4179. PMID:16593056 Page seeded by OCA on Sat May 3 05:20:50 2008

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