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2l2p

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Revision as of 08:20, 25 July 2018

Folding Intermediate of the Fyn SH3 A39V/N53P/V55L from NMR Relaxation Dispersion Experiments

Structural highlights

2l2p is a 1 chain structure with sequence from Chick. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1shf, 3cqt, 2lp5
Gene:	FYN (CHICK)
Activity:	Non-specific protein-tyrosine kinase, with EC number 2.7.10.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1]

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^[2]

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

References

↑ Zisch AH, D'Alessandri L, Amrein K, Ranscht B, Winterhalter KH, Vaughan L. The glypiated neuronal cell adhesion molecule contactin/F11 complexes with src-family protein tyrosine kinase Fyn. Mol Cell Neurosci. 1995 Jun;6(3):263-79. PMID:7496631 doi:http://dx.doi.org/S1044-7431(85)71021-4
↑ Neudecker P, Robustelli P, Cavalli A, Walsh P, Lundstrom P, Zarrine-Afsar A, Sharpe S, Vendruscolo M, Kay LE. Structure of an intermediate state in protein folding and aggregation. Science. 2012 Apr 20;336(6079):362-6. PMID:22517863 doi:10.1126/science.1214203

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2l2p"

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 ==Folding Intermediate of the Fyn SH3 A39V/N53P/V55L from NMR Relaxation Dispersion Experiments==
 <StructureSection load='2l2p' size='340' side='right' caption='[[2l2p]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
@@ Line 6: / Line 7: @@
 <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 CHICK])</td></tr>
 <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 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=2l2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l2p OCA], [http://pdbe.org/2l2p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l2p RCSB], [http://www.ebi.ac.uk/pdbsum/2l2p 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=2l2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l2p OCA], [http://pdbe.org/2l2p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l2p RCSB], [http://www.ebi.ac.uk/pdbsum/2l2p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l2p ProSAT]</span></td></tr>
 </table>
 == Function ==

2l2p

From Proteopedia

Revision as of 08:20, 25 July 2018

Folding Intermediate of the Fyn SH3 A39V/N53P/V55L from NMR Relaxation Dispersion Experiments

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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