5vf1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5vf1 is ON HOLD until Paper Publication
+
==X-ray Crystallographic Structure of a Giant Double-Walled Peptide Nanotube Formed by a Macrocyclic Beta-Sheet Containing ABeta16-22==
 +
<StructureSection load='5vf1' size='340' side='right' caption='[[5vf1]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[5vf1]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VF1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VF1 FirstGlance]. <br>
 +
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MEA:N-METHYLPHENYLALANINE'>MEA</scene>, <scene name='pdbligand=ORN:L-ORNITHINE'>ORN</scene>, <scene name='pdbligand=PHI:IODO-PHENYLALANINE'>PHI</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5vf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vf1 OCA], [http://pdbe.org/5vf1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vf1 RCSB], [http://www.ebi.ac.uk/pdbsum/5vf1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vf1 ProSAT]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
This paper describes the supramolecular assembly of a macrocyclic beta-sheet containing residues 16-22 of the beta-amyloid peptide, Abeta. X-ray crystallography reveals that the macrocyclic beta-sheet assembles to form double-walled nanotubes, with an inner diameter of 7 nm and outer diameter of 11 nm. The inner wall is composed of an extended network of hydrogen-bonded dimers. The outer wall is composed of a separate extended network of beta-barrel-like tetramers. These large peptide nanotubes pack into a hexagonal lattice that resembles a honeycomb. The complexity and size of the peptide nanotubes rivals some of the largest tubular biomolecular assemblies, such as GroEL and microtubules. These observations demonstrate that small amyloidogenic sequences can be used to build large nanostructures.
-
Authors:
+
X-ray Crystallographic Structure of a Giant Double-Walled Peptide Nanotube Formed by a Macrocyclic beta-Sheet Containing Abeta16-22.,Chen KH, Corro KA, Le SP, Nowick JS J Am Chem Soc. 2017 Jun 21;139(24):8102-8105. doi: 10.1021/jacs.7b03890. Epub, 2017 Jun 13. PMID:28598147<ref>PMID:28598147</ref>
-
Description:
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
 +
<div class="pdbe-citations 5vf1" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Chen, K H]]
 +
[[Category: Corro, K A]]
 +
[[Category: Le, S P]]
 +
[[Category: Nowick, J S]]
 +
[[Category: Amyloid-beta]]
 +
[[Category: De novo peptide design]]
 +
[[Category: De novo protein]]
 +
[[Category: Macrocyclic peptide]]
 +
[[Category: Nanotube]]

Revision as of 10:25, 27 September 2017

X-ray Crystallographic Structure of a Giant Double-Walled Peptide Nanotube Formed by a Macrocyclic Beta-Sheet Containing ABeta16-22

5vf1, resolution 2.10Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools