3u29

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3u29.png|left|200px]]
+
==Structural insights into charge pair interactions in triple helical proteins==
 +
<StructureSection load='3u29' size='340' side='right' caption='[[3u29]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3u29]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U29 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U29 FirstGlance]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene></td></tr>
 +
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t4f|3t4f]]</td></tr>
 +
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3u29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u29 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u29 RCSB], [http://www.ebi.ac.uk/pdbsum/3u29 PDBsum]</span></td></tr>
 +
<table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The collagen triple helix is the most abundant protein fold in humans. Despite its deceptively simple structure, very little is understood about its folding and fibrillization energy landscape. In this work, using a combination of x-ray crystallography and nuclear magnetic resonance spectroscopy, we carry out a detailed study of stabilizing pair-wise interactions between the positively charged lysine and the negatively charged amino acids aspartate and glutamate. We find important differences in the side chain conformation of amino acids in the crystalline and solution state. Structures from x-ray crystallography may have similarities to the densely packed triple helices of collagen fibers whereas solution NMR structures reveal the simpler interactions of isolated triple helices. In solution, two distinct types of contacts are observed: axial and lateral. Such register-specific interactions are crucial for the understanding of the registration process of collagens and the overall stability of proteins in this family. However, in the crystalline state, there is a significant rearrangement of the side chain conformation allowing for packing interactions between adjacent helices, which suggests that charged amino acids may play a dual role in collagen stabilization and folding, first at the level of triple helical assembly and second during fibril formation.
-
<!--
+
Structural insights into charge pair interactions in triple helical collagen-like proteins.,Fallas JA, Dong J, Tao YJ, Hartgerink JD J Biol Chem. 2012 Mar 9;287(11):8039-47. Epub 2011 Dec 17. PMID:22179819<ref>PMID:22179819</ref>
-
The line below this paragraph, containing "STRUCTURE_3u29", creates the "Structure Box" on the page.
+
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
-
or leave the SCENE parameter empty for the default display.
+
-
-->
+
-
{{STRUCTURE_3u29| PDB=3u29 | SCENE= }}
+
-
===Structural insights into charge pair interactions in triple helical proteins===
+
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
 
+
== References ==
-
<!--
+
<references/>
-
The line below this paragraph, {{ABSTRACT_PUBMED_22179819}}, adds the Publication Abstract to the page
+
__TOC__
-
(as it appears on PubMed at http://www.pubmed.gov), where 22179819 is the PubMed ID number.
+
</StructureSection>
-
-->
+
-
{{ABSTRACT_PUBMED_22179819}}
+
-
 
+
-
==About this Structure==
+
-
[[3u29]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U29 OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:022179819</ref><references group="xtra"/>
+
[[Category: Dong, J.]]
[[Category: Dong, J.]]
[[Category: Fallas, J A.]]
[[Category: Fallas, J A.]]

Revision as of 06:15, 5 June 2014

Structural insights into charge pair interactions in triple helical proteins

3u29, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3u29"
Views
Personal tools
Navigation
Toolbox