1ppt | pdb_00001ppt

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

spinqualitylabelsall models 1ppt, resolution 1.37Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ppt is a 1 chain structure with sequence from Melga. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PAHO_MELGA] Pancreatic hormone is synthesized in pancreatic islets of Langerhans and acts as a regulator of pancreatic and gastrointestinal functions. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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