View source for 2l2p


==Folding Intermediate of the Fyn SH3 A39V/N53P/V55L from NMR Relaxation Dispersion Experiments==
<StructureSection load='2l2p' size='340' side='right'caption='[[2l2p]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2l2p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L2P 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=2l2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l2p OCA], [https://pdbe.org/2l2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l2p RCSB], [https://www.ebi.ac.uk/pdbsum/2l2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l2p ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FYN_CHICK FYN_CHICK] Tyrosine-protein kinase implicated in the control of cell growth. Plays a role in the regulation of intracellular calcium levels. Required in brain development and mature brain function with important roles in the regulation of axon growth, axon guidance, and neurite extension. Role in CNTN1-mediated signaling.<ref>PMID:7496631</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein-folding intermediates have been implicated in amyloid fibril formation involved in neurodegenerative disorders. However, the structural mechanisms by which intermediates initiate fibrillar aggregation have remained largely elusive. To gain insight, we used relaxation dispersion nuclear magnetic resonance spectroscopy to determine the structure of a low-populated, on-pathway folding intermediate of the A39V/N53P/V55L (A, Ala; V, Val; N, Asn; P, Pro; L, Leu) Fyn SH3 domain. The carboxyl terminus remains disordered in this intermediate, thereby exposing the aggregation-prone amino-terminal beta strand. Accordingly, mutants lacking the carboxyl terminus and thus mimicking the intermediate fail to safeguard the folding route and spontaneously form fibrillar aggregates. The structure provides a detailed characterization of the non-native interactions stabilizing an aggregation-prone intermediate under native conditions and insight into how such an intermediate can derail folding and initiate fibrillation.

Structure of an intermediate state in protein folding and aggregation.,Neudecker P, Robustelli P, Cavalli A, Walsh P, Lundstrom P, Zarrine-Afsar A, Sharpe S, Vendruscolo M, Kay LE Science. 2012 Apr 20;336(6079):362-6. PMID:22517863<ref>PMID:22517863</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2l2p" style="background-color:#fffaf0;"></div>

==See Also==
*[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Cavalli A]]
[[Category: Kay LE]]
[[Category: Neudecker P]]
[[Category: Robustelli P]]
[[Category: Vendruscolo M]]