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.


1cgd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1cgd.gif|left|200px]]
[[Image:1cgd.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1cgd |SIZE=350|CAPTION= <scene name='initialview01'>1cgd</scene>, resolution 1.85&Aring;
+
The line below this paragraph, containing "STRUCTURE_1cgd", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1cgd| PDB=1cgd | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cgd OCA], [http://www.ebi.ac.uk/pdbsum/1cgd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cgd RCSB]</span>
+
-
}}
+
'''HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE'''
'''HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE'''
Line 19: Line 16:
==About this Structure==
==About this Structure==
-
1CGD is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CGD OCA].
+
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CGD OCA].
==Reference==
==Reference==
Hydration structure of a collagen peptide., Bella J, Brodsky B, Berman HM, Structure. 1995 Sep 15;3(9):893-906. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8535783 8535783]
Hydration structure of a collagen peptide., Bella J, Brodsky B, Berman HM, Structure. 1995 Sep 15;3(9):893-906. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8535783 8535783]
-
[[Category: Protein complex]]
 
[[Category: Bella, J.]]
[[Category: Bella, J.]]
[[Category: Berman, H M.]]
[[Category: Berman, H M.]]
[[Category: Brodsky, B.]]
[[Category: Brodsky, B.]]
-
[[Category: collagen]]
+
[[Category: Collagen]]
-
[[Category: collagen hydration]]
+
[[Category: Collagen hydration]]
-
[[Category: connective tissue]]
+
[[Category: Connective tissue]]
-
[[Category: extracellular matrix]]
+
[[Category: Extracellular matrix]]
-
[[Category: hydroxyproline]]
+
[[Category: Hydroxyproline]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:42:28 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:21:15 2008''
+

Revision as of 09:42, 2 May 2008

Template:STRUCTURE 1cgd

HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE


Overview

BACKGROUND: The collagen triple helix is a unique protein motif defined by the supercoiling of three polypeptide chains in a polyproline II conformation. It is a major domain of all collagen proteins and is also reported to exist in proteins with host defense function and in several membrane proteins. The triple-helical domain has distinctive properties. Collagen requires a high proportion of the post-translationally modified imino acid 4-hydroxyproline and water to stabilize its conformation and assembly. The crystal structure of a collagen-like peptide determined to 1.85 Angstrum showed that these two features may be related. RESULTS: A detailed analysis of the hydration structure of the collagen-like peptide is presented. The water molecules around the carbonyl and hydroxyprolyl groups show distinctive geometries. There are repetitive patterns of water bridges that link oxygen atoms within a single peptide chain, between different chains and between different triple helices. Overall, the water molecules are organized in a semi-clathrate-like structure that surrounds and interconnects triple helices in the crystal lattice. Hydroxyprolyl groups play a crucial role in the assembly. CONCLUSIONS: The roles of hydroxyproline and hydration are strongly interrelated in the structure of the collagen triple helix. The specific, repetitive water bridges observed in this structure buttress the triple-helical conformation. The extensively ordered hydration structure offers a good model for the interpretation of the experimental results on collagen stability and assembly.

About this Structure

Full crystallographic information is available from OCA.

Reference

Hydration structure of a collagen peptide., Bella J, Brodsky B, Berman HM, Structure. 1995 Sep 15;3(9):893-906. PMID:8535783 Page seeded by OCA on Fri May 2 12:42:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools