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| | <StructureSection load='3cqt' size='340' side='right'caption='[[3cqt]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='3cqt' size='340' side='right'caption='[[3cqt]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3cqt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CQT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3CQT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3cqt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CQT FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3cqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cqt OCA], [http://pdbe.org/3cqt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cqt RCSB], [http://www.ebi.ac.uk/pdbsum/3cqt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cqt ProSAT]</span></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=3cqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cqt OCA], [https://pdbe.org/3cqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cqt RCSB], [https://www.ebi.ac.uk/pdbsum/3cqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cqt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Gallus gallus]] | | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Non-specific protein-tyrosine kinase]]
| + | [[Category: Chan HS]] |
| - | [[Category: Chan, H S]] | + | [[Category: Davidson A]] |
| - | [[Category: Davidson, A]] | + | [[Category: Howell PL]] |
| - | [[Category: Howell, P L]] | + | [[Category: Neculai AM]] |
| - | [[Category: Neculai, A M]] | + | [[Category: Zarrine-Afsar A]] |
| - | [[Category: Zarrine-Afsar, A]] | + | |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Beta barrel]]
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| - | [[Category: Developmental protein]]
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| - | [[Category: Kinase]]
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| - | [[Category: Lipoprotein]]
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| - | [[Category: Manganese]]
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| - | [[Category: Metal-binding]]
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| - | [[Category: Myristate]]
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| - | [[Category: Nucleotide-binding]]
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| - | [[Category: Palmitate]]
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| - | [[Category: Phosphoprotein]]
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| - | [[Category: Proto-oncogene]]
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| - | [[Category: Sh2 domain]]
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| - | [[Category: Sh3 domain]]
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| - | [[Category: Transferase]]
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| - | [[Category: Tyrosine-protein kinase]]
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| Structural highlights
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]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Many experimental and theoretical studies have suggested a significant role for nonnative interactions in protein folding pathways, but the energetic contributions of these interactions are not well understood. We have addressed the energetics and the position specificity of nonnative hydrophobic interactions by developing a continuum coarse-grained chain model with a native-centric potential augmented by sequence-dependent hydrophobic interactions. By modeling the effect of different hydrophobicity values at various positions in the Fyn SH3 domain, we predicted energetically significant nonnative interactions that led to acceleration or deceleration of the folding rate depending on whether they were more populated in the transition state or unfolded state. These nonnative contacts were centered on position 53 in the Fyn SH3 domain, which lies in an exposed position in a 3(10)-helix. The energetic importance of the predicted nonnative interactions was confirmed experimentally by folding kinetics studies combined with double mutant thermodynamic cycles. By attaining agreement of theoretical and experimental investigations, this study provides a compelling demonstration that specific nonnative interactions can significantly influence folding energetics. Moreover, we show that a coarse-grained model with a simple consideration of hydrophobicity is sufficient for the accurate prediction of kinetically important nonnative interactions.
Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding.,Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR, Chan HS Proc Natl Acad Sci U S A. 2008 Jul 22;105(29):9999-10004. Epub 2008 Jul, 14. PMID:18626019[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
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
- ↑ Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, Davidson AR, Chan HS. Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci U S A. 2008 Jul 22;105(29):9999-10004. Epub 2008 Jul, 14. PMID:18626019
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