1jeg

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{{Seed}}
 
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[[Image:1jeg.png|left|200px]]
 
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==Solution structure of the SH3 domain from C-terminal Src Kinase complexed with a peptide from the tyrosine phosphatase PEP==
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The line below this paragraph, containing "STRUCTURE_1jeg", creates the "Structure Box" on the page.
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<StructureSection load='1jeg' size='340' side='right'caption='[[1jeg]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1jeg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JEG FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jeg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jeg OCA], [https://pdbe.org/1jeg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jeg RCSB], [https://www.ebi.ac.uk/pdbsum/1jeg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jeg ProSAT]</span></td></tr>
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{{STRUCTURE_1jeg| PDB=1jeg | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PTN22_MOUSE PTN22_MOUSE] Acts as negative regulator of T-cell receptor (TCR) signaling by direct dephosphorylation of the Src family kinases LCK and FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and other key signaling molecules. Associates with and probably dephosphorylates CBL. Dephosphorylates LCK at its activating 'Tyr-394' residue. Dephosphorylates ZAP70 at its activating 'Tyr-492' residue. Dephosphorylates the immune system activator SKAP2 (By similarity).<ref>PMID:8890164</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/je/1jeg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1jeg ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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C-terminal Src kinase (Csk) takes part in a highly specific, high affinity interaction via its Src homology 3 (SH3) domain with the proline-enriched tyrosine phosphatase PEP in hematopoietic cells. The solution structure of the Csk-SH3 domain in complex with a 25-residue peptide from the Pro/Glu/Ser/Thr-rich (PEST) domain of PEP reveals the basis for this specific peptide recognition motif involving an SH3 domain. Three residues, Ala 40, Thr 42 and Lys 43, in the SH3 domain of Csk specifically recognize two hydrophobic residues, Ile 625 and Val 626, in the proline-rich sequence of the PEST domain of PEP. These two residues are C-terminal to the conventional proline-rich SH3 domain recognition sequence of PEP. This interaction is required in addition to the classic polyproline helix (PPII) recognition by the Csk-SH3 domain for the association between Csk and PEP in vivo. NMR relaxation analysis suggests that Csk-SH3 has different dynamic properties in the various subsites important for peptide recognition.
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===Solution structure of the SH3 domain from C-terminal Src Kinase complexed with a peptide from the tyrosine phosphatase PEP===
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A novel, specific interaction involving the Csk SH3 domain and its natural ligand.,Ghose R, Shekhtman A, Goger MJ, Ji H, Cowburn D Nat Struct Biol. 2001 Nov;8(11):998-1004. PMID:11685249<ref>PMID:11685249</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1jeg" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11685249}}, adds the Publication Abstract to the page
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*[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 11685249 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11685249}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1JEG is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEG OCA].
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==Reference==
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<ref group="xtra">PMID:11685249</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Transferase]]
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[[Category: Cowburn D]]
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[[Category: Cowburn, D.]]
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[[Category: Ghose R]]
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[[Category: Ghose, R.]]
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[[Category: Goger MJ]]
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[[Category: Goger, M J.]]
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[[Category: Ji H]]
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[[Category: Ji, H.]]
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[[Category: Shekhtman A]]
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[[Category: Shekhtman, A.]]
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[[Category: Kinase]]
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[[Category: Protein-peptide complex]]
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[[Category: Sh3 domain]]
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[[Category: Tyrosine phosphatase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 15:36:13 2009''
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Current revision

Solution structure of the SH3 domain from C-terminal Src Kinase complexed with a peptide from the tyrosine phosphatase PEP

PDB ID 1jeg

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