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3pfv
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3pfv is ON HOLD Authors: Chaikuad, A., Guo, K., Cooper, C.D.O., Ayinampudi, V., Krojer, T., Muniz, J.R.C., Vollmar, M., Canning, P., Gileadi, O., vo...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Cbl-b TKB domain in complex with EGFR pY1069 peptide== | |
| + | <StructureSection load='3pfv' size='340' side='right'caption='[[3pfv]], [[Resolution|resolution]] 2.27Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3pfv]] is a 4 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=3PFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PFV FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.27Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3pfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pfv OCA], [https://pdbe.org/3pfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pfv RCSB], [https://www.ebi.ac.uk/pdbsum/3pfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pfv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CBLB_HUMAN CBLB_HUMAN] E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation. In activated T-cells, inhibits PLCG1 activation and calcium mobilization upon restimulation and promotes anergy. In B-cells, acts by ubiquitinating SYK and promoting its proteasomal degradation. May also be involved in EGFR ubiquitination and internalization.<ref>PMID:10022120</ref> <ref>PMID:10086340</ref> <ref>PMID:11087752</ref> <ref>PMID:11526404</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arrowsmith CH]] | ||
| + | [[Category: Ayinampudi V]] | ||
| + | [[Category: Bountra C]] | ||
| + | [[Category: Bullock A]] | ||
| + | [[Category: Canning P]] | ||
| + | [[Category: Chaikuad A]] | ||
| + | [[Category: Cooper CDO]] | ||
| + | [[Category: Edwards AM]] | ||
| + | [[Category: Gileadi O]] | ||
| + | [[Category: Guo K]] | ||
| + | [[Category: Krojer T]] | ||
| + | [[Category: Muniz JRC]] | ||
| + | [[Category: Vollmar M]] | ||
| + | [[Category: Weigelt J]] | ||
| + | [[Category: Von Delft F]] | ||
Current revision
Crystal structure of Cbl-b TKB domain in complex with EGFR pY1069 peptide
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Categories: Homo sapiens | Large Structures | Arrowsmith CH | Ayinampudi V | Bountra C | Bullock A | Canning P | Chaikuad A | Cooper CDO | Edwards AM | Gileadi O | Guo K | Krojer T | Muniz JRC | Vollmar M | Weigelt J | Von Delft F
