View source for 2mnu


==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]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mnu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2MNU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mnu OCA], [https://pdbe.org/2mnu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mnu RCSB], [https://www.ebi.ac.uk/pdbsum/2mnu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mnu ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN] Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:[https://omim.org/entry/601894 601894]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.<ref>PMID:18268355</ref> 
== Function ==
[https://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN] Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref>   Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref> 
<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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mnu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Suh J]]
[[Category: Yu T]]