This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ppt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ppt.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ppt.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ppt| PDB=1ppt | SCENE= }}
{{STRUCTURE_1ppt| PDB=1ppt | SCENE= }}
-
'''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===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16593056}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16593056 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16593056}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Wood, S P.]]
[[Category: Wood, S P.]]
[[Category: Pancreatic hormone]]
[[Category: Pancreatic hormone]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:20:50 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:51:56 2008''

Revision as of 09:51, 28 July 2008

Image:1ppt.png

Template:STRUCTURE 1ppt

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

Template:ABSTRACT PUBMED 16593056

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 Mon Jul 28 12:51:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ppt"
Personal tools