2mnu: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

==Backbone and side chain 1H, 13C, and 15N Chemical Shift Assignments for EDB and specific binding aptide==

== Structural highlights ==

<table><tr><td colspan='2'>[[2mnu]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MNU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MNU FirstGlance]. <br>

</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=2mnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mnu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mnu RCSB], [http://www.ebi.ac.uk/pdbsum/2mnu PDBsum]</span></td></tr>

<table>

== Publication Abstract from PubMed ==

Aptides, a novel class of high-affinity peptides, recognize diverse molecular targets with high affinity and specificity. The solution structure of the aptide APT specifically bound to fibronectin extradomain B (EDB), which represents an unusual protein-protein interaction that involves coupled unfolding and binding, is reported. APT binding is accompanied by unfolding of the C-terminal beta strand of EDB, thereby permitting APT to interact with the freshly exposed hydrophobic interior surfaces of EDB. The beta-hairpin scaffold of APT drives the interaction by a beta-strand displacement mechanism, such that an intramolecular beta sheet is replaced by an intermolecular beta sheet. The unfolding of EDB perturbs the tight domain association between EDB and FN8 of fibronectin, thus highlighting its potential use as a scaffold that switches between stretched and bent conformations.

~~The entry 2mnu is ON HOLD until Paper Publication~~

An Unusual Protein-Protein Interaction through Coupled Unfolding and Binding.,Yu TK, Shin SA, Kim EH, Kim S, Ryu KS, Cheong H, Ahn HC, Jon S, Suh JY Angew Chem Int Ed Engl. 2014 Sep 8;53(37):9784-7. doi: 10.1002/anie.201404750., Epub 2014 Jul 1. PMID:24985319<ref>PMID:24985319</ref>

~~Authors~~: Suh, J., Yu, T.

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~Description~~: ~~Backbone and side chain 1H, 13C, and 15N Chemical Shift Assignments for EDB and specific binding aptide~~

== References ==

__TOC__

</StructureSection>

[[Category: Suh, J.]]

[[Category: Yu, T.]]

[[Category: Aptide]]

[[Category: Cell adhesion]]

[[Category: Edb]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Backbone and side chain 1H, 13C, and 15N Chemical Shift Assignments for EDB and specific binding aptide==
+<StructureSection load='2mnu' size='340' side='right' caption='[[2mnu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2mnu]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MNU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MNU FirstGlance]. <br>
+</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=2mnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mnu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mnu RCSB], [http://www.ebi.ac.uk/pdbsum/2mnu PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Aptides, a novel class of high-affinity peptides, recognize diverse molecular targets with high affinity and specificity. The solution structure of the aptide APT specifically bound to fibronectin extradomain B (EDB), which represents an unusual protein-protein interaction that involves coupled unfolding and binding, is reported. APT binding is accompanied by unfolding of the C-terminal beta strand of EDB, thereby permitting APT to interact with the freshly exposed hydrophobic interior surfaces of EDB. The beta-hairpin scaffold of APT drives the interaction by a beta-strand displacement mechanism, such that an intramolecular beta sheet is replaced by an intermolecular beta sheet. The unfolding of EDB perturbs the tight domain association between EDB and FN8 of fibronectin, thus highlighting its potential use as a scaffold that switches between stretched and bent conformations.
-The entry 2mnu is ON HOLD  until Paper Publication
+An Unusual Protein-Protein Interaction through Coupled Unfolding and Binding.,Yu TK, Shin SA, Kim EH, Kim S, Ryu KS, Cheong H, Ahn HC, Jon S, Suh JY Angew Chem Int Ed Engl. 2014 Sep 8;53(37):9784-7. doi: 10.1002/anie.201404750., Epub 2014 Jul 1. PMID:24985319<ref>PMID:24985319</ref>
-Authors: Suh, J., Yu, T.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Backbone and side chain 1H, 13C, and 15N Chemical Shift Assignments for EDB and specific binding aptide
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Suh, J.]]
+[[Category: Yu, T.]]
+[[Category: Aptide]]
+[[Category: Cell adhesion]]
+[[Category: Edb]]