2lp5: Difference between revisions
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<StructureSection load='2lp5' size='340' side='right' caption='[[2lp5]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='2lp5' size='340' side='right' caption='[[2lp5]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2lp5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LP5 OCA]. <br> | <table><tr><td colspan='2'>[[2lp5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LP5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LP5 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1shf|1shf]], [[3cqt|3cqt]], [[2l2p|2l2p]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1shf|1shf]], [[3cqt|3cqt]], [[2l2p|2l2p]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FYN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FYN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus])</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_protein-tyrosine_kinase Non-specific protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.2 2.7.10.2] </span></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=2lp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lp5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lp5 RCSB], [http://www.ebi.ac.uk/pdbsum/2lp5 PDBsum]</span></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=2lp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lp5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lp5 RCSB], [http://www.ebi.ac.uk/pdbsum/2lp5 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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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> | 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 | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
==See Also== | |||
*[[Tyrosine kinase|Tyrosine kinase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 22: | Line 25: | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Non-specific protein-tyrosine kinase]] | [[Category: Non-specific protein-tyrosine kinase]] | ||
[[Category: Cavalli, A | [[Category: Cavalli, A]] | ||
[[Category: Kay, L E | [[Category: Kay, L E]] | ||
[[Category: Neudecker, P | [[Category: Neudecker, P]] | ||
[[Category: Robustelli, P | [[Category: Robustelli, P]] | ||
[[Category: Vendruscolo, M | [[Category: Vendruscolo, M]] | ||
[[Category: Amyloid fibril]] | [[Category: Amyloid fibril]] | ||
[[Category: Protein folding intermediate]] | [[Category: Protein folding intermediate]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 09:19, 22 December 2014
Native Structure of the Fyn SH3 A39V/N53P/V55LNative Structure of the Fyn SH3 A39V/N53P/V55L
Structural highlights
Publication Abstract from PubMedProtein-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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