2ydl

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Current revision (10:50, 20 December 2023) (edit) (undo)
 
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<StructureSection load='2ydl' size='340' side='right'caption='[[2ydl]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
<StructureSection load='2ydl' size='340' side='right'caption='[[2ydl]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ydl]] 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=2YDL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YDL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ydl]] 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=2YDL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YDL FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2bz8|2bz8]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</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=2ydl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ydl OCA], [https://pdbe.org/2ydl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ydl RCSB], [https://www.ebi.ac.uk/pdbsum/2ydl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ydl 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=2ydl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ydl OCA], [https://pdbe.org/2ydl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ydl RCSB], [https://www.ebi.ac.uk/pdbsum/2ydl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ydl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/SH3K1_HUMAN SH3K1_HUMAN]] Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through a association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit (By similarity). May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration.<ref>PMID:12177062</ref> <ref>PMID:11894095</ref> <ref>PMID:11894096</ref> <ref>PMID:12771190</ref> <ref>PMID:12734385</ref> <ref>PMID:15090612</ref> <ref>PMID:16256071</ref> <ref>PMID:15707590</ref> <ref>PMID:16177060</ref> <ref>PMID:21834987</ref>
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[https://www.uniprot.org/uniprot/SH3K1_HUMAN SH3K1_HUMAN] Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through a association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit (By similarity). May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration.<ref>PMID:12177062</ref> <ref>PMID:11894095</ref> <ref>PMID:11894096</ref> <ref>PMID:12771190</ref> <ref>PMID:12734385</ref> <ref>PMID:15090612</ref> <ref>PMID:16256071</ref> <ref>PMID:15707590</ref> <ref>PMID:16177060</ref> <ref>PMID:21834987</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bravo, J]]
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[[Category: Bravo J]]
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[[Category: Cardenes, N]]
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[[Category: Cardenes N]]
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[[Category: Signaling protein]]
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Current revision

Crystal structure of SH3C from CIN85

PDB ID 2ydl

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