1a3j: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,567 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,567 edits
No edit summary
Line 1: Line 1:
[[Image:1a3j.gif|left|200px]]
{{Seed}}
[[Image:1a3j.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1a3j|  PDB=1a3j  |  SCENE=  }}  
{{STRUCTURE_1a3j|  PDB=1a3j  |  SCENE=  }}  


'''X-RAY CRYSTALLOGRAPHIC DETERMINATION OF A COLLAGEN-LIKE PEPTIDE WITH THE REPEATING SEQUENCE (PRO-PRO-GLY)'''
===X-RAY CRYSTALLOGRAPHIC DETERMINATION OF A COLLAGEN-LIKE PEPTIDE WITH THE REPEATING SEQUENCE (PRO-PRO-GLY)===




==Overview==
<!--
The crystal structure of the triple-helical peptide (Pro-Pro-Gly)10 has been re-determined to obtain a more accurate description for this widely studied collagen model and to provide a comparison with the recent high-resolution crystal structure of a collagen-like peptide containing Pro-Hyp-Gly regions. This structure demonstrated that hydroxyproline participates extensively in a repetitive hydrogen-bonded assembly between the peptide and the solvent molecules. Two separate structural studies of the peptide (Pro-Pro-Gly)10 were performed with different crystallization conditions, data collection temperatures, and X-ray sources. The polymer-like structure of one triple-helical repeat of Pro-Pro-Gly has been determined to 2.0 A resolution in one case and 1.7 A resolution in the other. The solvent structures of the two peptides were independently determined specifically for validation purposes. The two structures display a reverse chain trace compared with the original structure determination. In comparison with the Hyp-containing peptide, the two Pro-Pro-Gly structures demonstrate very similar molecular conformation and analogous hydration patterns involving carbonyl groups, but have different crystal packing. This difference in crystal packing indicates that the involvement of hydroxyproline in an extended hydration network is critical for the lateral assembly and supermolecular structure of collagen.
The line below this paragraph, {{ABSTRACT_PUBMED_9677293}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9677293 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_9677293}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Collagen]]
[[Category: Collagen]]
[[Category: Extracellular matrix]]
[[Category: Extracellular matrix]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:45:29 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:55:44 2008''

Revision as of 12:55, 30 June 2008

File:1a3j.png

Template:STRUCTURE 1a3j

X-RAY CRYSTALLOGRAPHIC DETERMINATION OF A COLLAGEN-LIKE PEPTIDE WITH THE REPEATING SEQUENCE (PRO-PRO-GLY)

Template:ABSTRACT PUBMED 9677293

About this Structure

Full crystallographic information is available from OCA.

Reference

X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly)., Kramer RZ, Vitagliano L, Bella J, Berisio R, Mazzarella L, Brodsky B, Zagari A, Berman HM, J Mol Biol. 1998 Jul 24;280(4):623-38. PMID:9677293

Page seeded by OCA on Mon Jun 30 15:55:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1a3j&oldid=570767"