|
|
(10 intermediate revisions not shown.) |
Line 1: |
Line 1: |
- | {{Seed}} | |
- | [[Image:2hda.png|left|200px]] | |
| | | |
- | <!-- | + | ==Yes SH3 domain== |
- | The line below this paragraph, containing "STRUCTURE_2hda", creates the "Structure Box" on the page.
| + | <StructureSection load='2hda' size='340' side='right'caption='[[2hda]], [[Resolution|resolution]] 1.90Å' scene=''> |
- | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[2hda]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HDA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HDA FirstGlance]. <br> |
- | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
- | -->
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
- | {{STRUCTURE_2hda| PDB=2hda | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hda OCA], [https://pdbe.org/2hda PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hda RCSB], [https://www.ebi.ac.uk/pdbsum/2hda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hda ProSAT]</span></td></tr> |
| + | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/YES_HUMAN YES_HUMAN] Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis.<ref>PMID:11901164</ref> <ref>PMID:17053785</ref> <ref>PMID:18479465</ref> <ref>PMID:19276087</ref> <ref>PMID:21566460</ref> <ref>PMID:21713032</ref> |
| + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> |
| + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hd/2hda_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| + | </jmolCheckbox> |
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hda ConSurf]. |
| + | <div style="clear:both"></div> |
| + | <div style="background-color:#fffaf0;"> |
| + | == Publication Abstract from PubMed == |
| + | SH3 domains from the Src family of tyrosine kinases represent an interesting example of the delicate balance between promiscuity and specificity characteristic of proline-rich ligand recognition by SH3 domains. The development of inhibitors of therapeutic potential requires a good understanding of the molecular determinants of binding affinity and specificity and relies on the availability of high quality structural information. Here, we present the first high-resolution crystal structure of the SH3 domain of the c-Yes oncogen. Comparison with other SH3 domains from the Src family revealed significant deviations in the loop regions. In particular, the n-Src loop, highly flexible and partially disordered, is stabilized in an unusual conformation by the establishment of several intramolecular hydrogen bonds. Additionally, we present here the first report of amyloid aggregation by an SH3 domain from the Src family. |
| | | |
- | ===Yes SH3 domain===
| + | Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: loop flexibility and amyloid aggregation.,Martin-Garcia JM, Luque I, Mateo PL, Ruiz-Sanz J, Camara-Artigas A FEBS Lett. 2007 May 1;581(9):1701-6. Epub 2007 Mar 30. PMID:17418139<ref>PMID:17418139</ref> |
| | | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> |
| + | <div class="pdbe-citations 2hda" style="background-color:#fffaf0;"></div> |
| | | |
- | <!--
| + | ==See Also== |
- | The line below this paragraph, {{ABSTRACT_PUBMED_17418139}}, adds the Publication Abstract to the page
| + | *[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]] |
- | (as it appears on PubMed at http://www.pubmed.gov), where 17418139 is the PubMed ID number.
| + | == References == |
- | -->
| + | <references/> |
- | {{ABSTRACT_PUBMED_17418139}}
| + | __TOC__ |
- | | + | </StructureSection> |
- | ==About this Structure== | + | |
- | 2HDA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HDA OCA].
| + | |
- | | + | |
- | ==Reference== | + | |
- | Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: loop flexibility and amyloid aggregation., Martin-Garcia JM, Luque I, Mateo PL, Ruiz-Sanz J, Camara-Artigas A, FEBS Lett. 2007 May 1;581(9):1701-6. Epub 2007 Mar 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17418139 17418139]
| + | |
| [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
- | [[Category: Non-specific protein-tyrosine kinase]] | + | [[Category: Large Structures]] |
- | [[Category: Single protein]]
| + | [[Category: Camara-Artigas A]] |
- | [[Category: Camara-Artigas, A.]] | + | [[Category: Luque I]] |
- | [[Category: Luque, I.]] | + | [[Category: Martin-Garcia JM]] |
- | [[Category: Martin-Garcia, J M.]] | + | [[Category: Mateo PL]] |
- | [[Category: Mateo, P L.]] | + | [[Category: Ruiz-Sanz J]] |
- | [[Category: Ruiz-Sanz, J.]] | + | |
- | [[Category: Main beta]]
| + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:25:38 2008''
| + | |
| Structural highlights
Function
YES_HUMAN Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis.[1] [2] [3] [4] [5] [6]
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
SH3 domains from the Src family of tyrosine kinases represent an interesting example of the delicate balance between promiscuity and specificity characteristic of proline-rich ligand recognition by SH3 domains. The development of inhibitors of therapeutic potential requires a good understanding of the molecular determinants of binding affinity and specificity and relies on the availability of high quality structural information. Here, we present the first high-resolution crystal structure of the SH3 domain of the c-Yes oncogen. Comparison with other SH3 domains from the Src family revealed significant deviations in the loop regions. In particular, the n-Src loop, highly flexible and partially disordered, is stabilized in an unusual conformation by the establishment of several intramolecular hydrogen bonds. Additionally, we present here the first report of amyloid aggregation by an SH3 domain from the Src family.
Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: loop flexibility and amyloid aggregation.,Martin-Garcia JM, Luque I, Mateo PL, Ruiz-Sanz J, Camara-Artigas A FEBS Lett. 2007 May 1;581(9):1701-6. Epub 2007 Mar 30. PMID:17418139[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lee SW, Bonnah RA, Higashi DL, Atkinson JP, Milgram SL, So M. CD46 is phosphorylated at tyrosine 354 upon infection of epithelial cells by Neisseria gonorrhoeae. J Cell Biol. 2002 Mar 18;156(6):951-7. Epub 2002 Mar 18. PMID:11901164 doi:10.1083/jcb.200109005
- ↑ Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z. Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. PMID:17053785 doi:7601384
- ↑ Martin NG, McAndrew PC, Eve PD, Garrett MD. Phosphorylation of cyclin dependent kinase 4 on tyrosine 17 is mediated by Src family kinases. FEBS J. 2008 Jun;275(12):3099-109. doi: 10.1111/j.1742-4658.2008.06463.x. Epub, 2008 May 8. PMID:18479465 doi:10.1111/j.1742-4658.2008.06463.x
- ↑ Varrin-Doyer M, Vincent P, Cavagna S, Auvergnon N, Noraz N, Rogemond V, Honnorat J, Moradi-Ameli M, Giraudon P. Phosphorylation of collapsin response mediator protein 2 on Tyr-479 regulates CXCL12-induced T lymphocyte migration. J Biol Chem. 2009 May 8;284(19):13265-76. doi: 10.1074/jbc.M807664200. Epub 2009 , Mar 10. PMID:19276087 doi:10.1074/jbc.M807664200
- ↑ Jung J, Lee MK, Jin Y, Fu SB, Rosales JL, Lee KY. Clues for c-Yes involvement in the cell cycle and cytokinesis. Cell Cycle. 2011 May 1;10(9):1502-3. Epub 2011 May 1. PMID:21566460
- ↑ Tauzin S, Chaigne-Delalande B, Selva E, Khadra N, Daburon S, Contin-Bordes C, Blanco P, Le Seyec J, Ducret T, Counillon L, Moreau JF, Hofman P, Vacher P, Legembre P. The naturally processed CD95L elicits a c-yes/calcium/PI3K-driven cell migration pathway. PLoS Biol. 2011 Jun;9(6):e1001090. doi: 10.1371/journal.pbio.1001090. Epub 2011, Jun 21. PMID:21713032 doi:10.1371/journal.pbio.1001090
- ↑ Martin-Garcia JM, Luque I, Mateo PL, Ruiz-Sanz J, Camara-Artigas A. Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: loop flexibility and amyloid aggregation. FEBS Lett. 2007 May 1;581(9):1701-6. Epub 2007 Mar 30. PMID:17418139 doi:10.1016/j.febslet.2007.03.059
|