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| ==Solution structure of the SH2 domain from mouse B-cell linker protein BLNK== | | ==Solution structure of the SH2 domain from mouse B-cell linker protein BLNK== |
- | <StructureSection load='2eo6' size='340' side='right' caption='[[2eo6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2eo6' size='340' side='right'caption='[[2eo6]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2eo6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EO6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EO6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2eo6]] is a 1 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=2EO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EO6 FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Blnk ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
- | <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=2eo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eo6 OCA], [http://pdbe.org/2eo6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2eo6 RCSB], [http://www.ebi.ac.uk/pdbsum/2eo6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2eo6 ProSAT], [http://www.topsan.org/Proteins/RSGI/2eo6 TOPSAN]</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=2eo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eo6 OCA], [https://pdbe.org/2eo6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eo6 RCSB], [https://www.ebi.ac.uk/pdbsum/2eo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eo6 ProSAT], [https://www.topsan.org/Proteins/RSGI/2eo6 TOPSAN]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/BLNK_MOUSE BLNK_MOUSE]] Functions as a central linker protein, downstream of the B-cell receptor (BCR), bridging the SYK kinase to a multitude of signaling pathways and regulating biological outcomes of B-cell function and development. Plays a role in the activation of ERK/EPHB2, MAP kinase p38 and JNK. Modulates AP1 activation. Important for the activation of NF-kappa-B and NFAT. Plays an important role in BCR-mediated PLCG1 and PLCG2 activation and Ca(2+) mobilization and is required for trafficking of the BCR to late endosomes. However, does not seem to be required for pre-BCR-mediated activation of MAP kinase and phosphatidyl-inositol 3 (PI3) kinase signaling. May be required for the RAC1-JNK pathway. Plays a critical role in orchestrating the pro-B cell to pre-B cell transition. May play an important role in BCR-induced B-cell apoptosis.<ref>PMID:9705962</ref> <ref>PMID:12761551</ref> <ref>PMID:18369315</ref> | + | [https://www.uniprot.org/uniprot/BLNK_MOUSE BLNK_MOUSE] Functions as a central linker protein, downstream of the B-cell receptor (BCR), bridging the SYK kinase to a multitude of signaling pathways and regulating biological outcomes of B-cell function and development. Plays a role in the activation of ERK/EPHB2, MAP kinase p38 and JNK. Modulates AP1 activation. Important for the activation of NF-kappa-B and NFAT. Plays an important role in BCR-mediated PLCG1 and PLCG2 activation and Ca(2+) mobilization and is required for trafficking of the BCR to late endosomes. However, does not seem to be required for pre-BCR-mediated activation of MAP kinase and phosphatidyl-inositol 3 (PI3) kinase signaling. May be required for the RAC1-JNK pathway. Plays a critical role in orchestrating the pro-B cell to pre-B cell transition. May play an important role in BCR-induced B-cell apoptosis.<ref>PMID:9705962</ref> <ref>PMID:12761551</ref> <ref>PMID:18369315</ref> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
- | [[Category: Hayashi, F]] | + | [[Category: Mus musculus]] |
- | [[Category: Kurosaki, C]] | + | [[Category: Hayashi F]] |
- | [[Category: Structural genomic]] | + | [[Category: Kurosaki C]] |
- | [[Category: Sano, R]] | + | [[Category: Sano R]] |
- | [[Category: Yokoyama, S]] | + | [[Category: Yokoyama S]] |
- | [[Category: Yoshida, M]] | + | [[Category: Yoshida M]] |
- | [[Category: B-cell adapter containing sh2 domain protein]]
| + | |
- | [[Category: B-cell adapter containing src homology 2 domain protein]]
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- | [[Category: Cytoplasmic adapter protein]]
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- | [[Category: Lymphocyte antigen 57]]
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- | [[Category: National project on protein structural and functional analyse]]
| + | |
- | [[Category: Nppsfa]]
| + | |
- | [[Category: Rsgi]]
| + | |
- | [[Category: Sh2]]
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- | [[Category: Signaling protein]]
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- | [[Category: Slp-65]]
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- | [[Category: Src homology 2 domain-containing leukocyte protein of 65 kda]]
| + | |
| Structural highlights
Function
BLNK_MOUSE Functions as a central linker protein, downstream of the B-cell receptor (BCR), bridging the SYK kinase to a multitude of signaling pathways and regulating biological outcomes of B-cell function and development. Plays a role in the activation of ERK/EPHB2, MAP kinase p38 and JNK. Modulates AP1 activation. Important for the activation of NF-kappa-B and NFAT. Plays an important role in BCR-mediated PLCG1 and PLCG2 activation and Ca(2+) mobilization and is required for trafficking of the BCR to late endosomes. However, does not seem to be required for pre-BCR-mediated activation of MAP kinase and phosphatidyl-inositol 3 (PI3) kinase signaling. May be required for the RAC1-JNK pathway. Plays a critical role in orchestrating the pro-B cell to pre-B cell transition. May play an important role in BCR-induced B-cell apoptosis.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Wienands J, Schweikert J, Wollscheid B, Jumaa H, Nielsen PJ, Reth M. SLP-65: a new signaling component in B lymphocytes which requires expression of the antigen receptor for phosphorylation. J Exp Med. 1998 Aug 17;188(4):791-5. PMID:9705962
- ↑ Jumaa H, Bossaller L, Portugal K, Storch B, Lotz M, Flemming A, Schrappe M, Postila V, Riikonen P, Pelkonen J, Niemeyer CM, Reth M. Deficiency of the adaptor SLP-65 in pre-B-cell acute lymphoblastic leukaemia. Nature. 2003 May 22;423(6938):452-6. PMID:12761551 doi:http://dx.doi.org/10.1038/nature01608
- ↑ Kulathu Y, Hobeika E, Turchinovich G, Reth M. The kinase Syk as an adaptor controlling sustained calcium signalling and B-cell development. EMBO J. 2008 May 7;27(9):1333-44. doi: 10.1038/emboj.2008.62. Epub 2008 Mar 27. PMID:18369315 doi:http://dx.doi.org/10.1038/emboj.2008.62
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