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.


2cuo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2cuo.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2cuo.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2cuo| PDB=2cuo | SCENE= }}
{{STRUCTURE_2cuo| PDB=2cuo | SCENE= }}
-
'''Collagen model peptide (PRO-PRO-GLY)9'''
+
===Collagen model peptide (PRO-PRO-GLY)9===
-
==Overview==
+
<!--
-
The crystal structure of a collagen-model peptide [(Pro-Pro-Gly)(9)](3) has been determined at 1.33 A resolution. Diffraction data were collected at 100 K using synchrotron radiation, which led to the first structural study of [(Pro-Pro-Gly)(n)](3) under cryogenic conditions. The crystals belong to the P2(1) space group with cell parameters of a = 25.95, b = 26.56, c = 80.14 Angstroms and beta = 90.0 degrees. The overall molecular conformation was consistent with the left-handed 7/2-helical model with an axial repeat of 20 A for native collagen. A total of 332 water molecules were found in an asymmetric unit. Proline residues in adjacent triple-helices exhibited three types of hydrophobic interactions. Furthermore, three types of hydrogen-bonding networks mediated by water molecules were observed between adjacent triple-helices. These hydrophobic interactions and hydrogen-bonding networks occurred at intervals of 20 Angstroms along the c-axis based on the previous sub-cell structures [(Pro-Pro-Gly)(n)](3) (n = 9, 10), which were also seen in the full-cell structure of [(Pro-Pro-Gly)(10)](3). Five proline residues at the Y position in the X-Y-Gly triplet were found in a down-puckering conformation, this being inconsistent with the recently proposed propensity-based hypothesis. These proline residues were forced to adopt opposing puckering because of the prevailing hydrophobic interaction between triple-helices compared with the Pro:Pro stacking interaction within a triple-helix.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16091587}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16091587 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16091587}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Puckering]]
[[Category: Puckering]]
[[Category: Triple-helix]]
[[Category: Triple-helix]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:06:40 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:05:15 2008''

Revision as of 22:05, 28 July 2008

Template:STRUCTURE 2cuo

Collagen model peptide (PRO-PRO-GLY)9

Template:ABSTRACT PUBMED 16091587

About this Structure

Full crystallographic information is available from OCA.

Reference

Repetitive interactions observed in the crystal structure of a collagen-model peptide, [(Pro-Pro-Gly)9]3., Hongo C, Noguchi K, Okuyama K, Tanaka Y, Nishino N, J Biochem. 2005 Aug;138(2):135-44. PMID:16091587

Page seeded by OCA on Tue Jul 29 01:05:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools