3khq: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3khq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KHQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KHQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[3khq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KHQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KHQ FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kg5|3kg5]], [[3kho|3kho]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kg5|3kg5]], [[3kho|3kho]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cd79b, Igb ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cd79b, Igb ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3khq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3khq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3khq RCSB], [http://www.ebi.ac.uk/pdbsum/3khq PDBsum]</span></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=3khq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3khq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3khq RCSB], [http://www.ebi.ac.uk/pdbsum/3khq PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/CD79B_MOUSE CD79B_MOUSE]] Required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation.<ref>PMID:8175787</ref> <ref>PMID:10352267</ref> <ref>PMID:12356683</ref> <ref>PMID:15661879</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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Structural and functional studies of Igalphabeta and its assembly with the B cell antigen receptor.,Radaev S, Zou Z, Tolar P, Nguyen K, Nguyen A, Krueger PD, Stutzman N, Pierce S, Sun PD Structure. 2010 Aug 11;18(8):934-43. PMID:20696394<ref>PMID:20696394</ref> | Structural and functional studies of Igalphabeta and its assembly with the B cell antigen receptor.,Radaev S, Zou Z, Tolar P, Nguyen K, Nguyen A, Krueger PD, Stutzman N, Pierce S, Sun PD Structure. 2010 Aug 11;18(8):934-43. PMID:20696394<ref>PMID:20696394</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Radaev, S | [[Category: Radaev, S]] | ||
[[Category: Sun, P D | [[Category: Sun, P D]] | ||
[[Category: Bcr]] | [[Category: Bcr]] | ||
[[Category: Cd79a]] | [[Category: Cd79a]] | ||
Revision as of 09:56, 25 December 2014
Crystal structure of murine Ig-beta (CD79b) in the monomeric formCrystal structure of murine Ig-beta (CD79b) in the monomeric form
Structural highlights
Function[CD79B_MOUSE] Required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation.[1] [2] [3] [4] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe B cell antigen receptor (BCR) plays an essential role in all phases of B cell development. Here we show that the extracellular domains of murine and human Igbeta form an I-set immunoglobulin-like structure with an interchain disulfide between cysteines on their G strands. Structural and sequence analysis suggests that Igalpha displays a similar fold as Igbeta. An Igalphabeta heterodimer model was generated based on the unique disulfide-bonded Igbeta dimer. Solution binding studies showed that the extracellular domains of Igalphabeta preferentially recognize the constant region of BCR with mu chain specificity, suggesting a role for Igalphabeta to enhance BCRmu chain signaling. Cluster mutations on Igalpha, Igbeta, and a membrane-bound form of immunoglobulin (mIgM) based on the structural model identified distinct areas of potential contacts involving charged residues on both subunits of the coreceptor and the Cmu4 domain of mIgM. These studies provide the first structural model for understanding BCR function. Structural and functional studies of Igalphabeta and its assembly with the B cell antigen receptor.,Radaev S, Zou Z, Tolar P, Nguyen K, Nguyen A, Krueger PD, Stutzman N, Pierce S, Sun PD Structure. 2010 Aug 11;18(8):934-43. PMID:20696394[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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