4tzi

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==Structure of unliganded Lyn SH2 domain==
==Structure of unliganded Lyn SH2 domain==
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<StructureSection load='4tzi' size='340' side='right' caption='[[4tzi]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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<StructureSection load='4tzi' size='340' side='right'caption='[[4tzi]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4tzi]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TZI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TZI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4tzi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TZI FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_protein-tyrosine_kinase Non-specific protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.2 2.7.10.2] </span></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]] 2.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tzi OCA], [http://pdbe.org/4tzi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tzi RCSB], [http://www.ebi.ac.uk/pdbsum/4tzi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tzi ProSAT]</span></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=4tzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tzi OCA], [https://pdbe.org/4tzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tzi RCSB], [https://www.ebi.ac.uk/pdbsum/4tzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tzi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/LYN_MOUSE LYN_MOUSE]] Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, PTK2B/PYK2, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr-72'.<ref>PMID:15335855</ref> <ref>PMID:7513017</ref> <ref>PMID:8128248</ref> <ref>PMID:7585947</ref> <ref>PMID:7584145</ref> <ref>PMID:8621063</ref> <ref>PMID:9064343</ref> <ref>PMID:8629002</ref> <ref>PMID:9252121</ref> <ref>PMID:9036984</ref> <ref>PMID:9573010</ref> <ref>PMID:9601638</ref> <ref>PMID:9480991</ref> <ref>PMID:9547345</ref> <ref>PMID:9469421</ref> <ref>PMID:9590210</ref> <ref>PMID:10594694</ref> <ref>PMID:10327049</ref> <ref>PMID:10672044</ref> <ref>PMID:10640270</ref> <ref>PMID:11007759</ref> <ref>PMID:11435302</ref> <ref>PMID:11672542</ref> <ref>PMID:12077122</ref> <ref>PMID:12874221</ref> <ref>PMID:14726379</ref> <ref>PMID:14525964</ref> <ref>PMID:16116174</ref> <ref>PMID:16034130</ref> <ref>PMID:16272347</ref> <ref>PMID:16249387</ref> <ref>PMID:16731527</ref> <ref>PMID:17640867</ref> <ref>PMID:19492092</ref> <ref>PMID:20189992</ref> <ref>PMID:20385881</ref>
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[https://www.uniprot.org/uniprot/LYN_MOUSE LYN_MOUSE] Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, PTK2B/PYK2, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr-72'.<ref>PMID:15335855</ref> <ref>PMID:7513017</ref> <ref>PMID:8128248</ref> <ref>PMID:7585947</ref> <ref>PMID:7584145</ref> <ref>PMID:8621063</ref> <ref>PMID:9064343</ref> <ref>PMID:8629002</ref> <ref>PMID:9252121</ref> <ref>PMID:9036984</ref> <ref>PMID:9573010</ref> <ref>PMID:9601638</ref> <ref>PMID:9480991</ref> <ref>PMID:9547345</ref> <ref>PMID:9469421</ref> <ref>PMID:9590210</ref> <ref>PMID:10594694</ref> <ref>PMID:10327049</ref> <ref>PMID:10672044</ref> <ref>PMID:10640270</ref> <ref>PMID:11007759</ref> <ref>PMID:11435302</ref> <ref>PMID:11672542</ref> <ref>PMID:12077122</ref> <ref>PMID:12874221</ref> <ref>PMID:14726379</ref> <ref>PMID:14525964</ref> <ref>PMID:16116174</ref> <ref>PMID:16034130</ref> <ref>PMID:16272347</ref> <ref>PMID:16249387</ref> <ref>PMID:16731527</ref> <ref>PMID:17640867</ref> <ref>PMID:19492092</ref> <ref>PMID:20189992</ref> <ref>PMID:20385881</ref>
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
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*[[Tyrosine kinase|Tyrosine kinase]]
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*[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Non-specific protein-tyrosine kinase]]
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[[Category: Large Structures]]
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[[Category: Wybenga-Groot, L E]]
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[[Category: Mus musculus]]
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[[Category: Sh2 domain]]
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[[Category: Wybenga-Groot LE]]
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[[Category: Transferase]]
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Current revision

Structure of unliganded Lyn SH2 domain

PDB ID 4tzi

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