2hda

From Proteopedia

(Difference between revisions)

Current revision

Yes SH3 domain

Structural highlights

2hda is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='2hda' size='340' side='right'caption='[[2hda]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2hda]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
+<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>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YES1, YES ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_protein-tyrosine_kinase Non-specific protein-tyrosine kinase], with EC number [https://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'>[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>
+[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]]
@@ Line 37: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Non-specific protein-tyrosine kinase]]
+[[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]]
-[[Category: Transferase]]

2hda

From Proteopedia

Current revision

Yes SH3 domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox