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