3khq: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(5 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:3khq.png|left|200px]]


<!--
==Crystal structure of murine Ig-beta (CD79b) in the monomeric form==
The line below this paragraph, containing "STRUCTURE_3khq", creates the "Structure Box" on the page.
<StructureSection load='3khq' size='340' side='right'caption='[[3khq]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3khq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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>
or leave the SCENE parameter empty for the default display.
</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 id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kg5|3kg5]], [[3kho|3kho]]</td></tr>
{{STRUCTURE_3khq|  PDB=3khq  |  SCENE= }}
<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 LK3 transgenic mice])</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://pdbe.org/3khq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3khq RCSB], [http://www.ebi.ac.uk/pdbsum/3khq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3khq ProSAT]</span></td></tr>
</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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kh/3khq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3khq ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 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.


===Crystal structure of murine Ig-beta (CD79b) in the monomeric form===
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 MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<!--
</div>
The line below this paragraph, {{ABSTRACT_PUBMED_20696394}}, adds the Publication Abstract to the page
<div class="pdbe-citations 3khq" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 20696394 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_20696394}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
[[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].
[[Category: Lk3 transgenic mice]]
 
[[Category: Radaev, S]]
==Reference==
[[Category: Sun, P D]]
<ref group="xtra">PMID:020696394</ref><references group="xtra"/>
[[Category: Mus musculus]]
[[Category: Radaev, S.]]
[[Category: Sun, P D.]]
[[Category: Bcr]]
[[Category: Bcr]]
[[Category: Cd79a]]
[[Category: Cd79a]]

Latest revision as of 14:08, 17 July 2019

Crystal structure of murine Ig-beta (CD79b) in the monomeric formCrystal structure of murine Ig-beta (CD79b) in the monomeric form

Structural highlights

3khq is a 1 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:Cd79b, Igb (LK3 transgenic mice)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

The 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

  1. ↑ Taddie JA, Hurley TR, Hardwick BS, Sefton BM. Activation of B- and T-cells by the cytoplasmic domains of the B-cell antigen receptor proteins Ig-alpha and Ig-beta. J Biol Chem. 1994 May 6;269(18):13529-35. PMID:8175787
  2. ↑ Siemasko K, Eisfelder BJ, Stebbins C, Kabak S, Sant AJ, Song W, Clark MR. Ig alpha and Ig beta are required for efficient trafficking to late endosomes and to enhance antigen presentation. J Immunol. 1999 Jun 1;162(11):6518-25. PMID:10352267
  3. ↑ Li C, Siemasko K, Clark MR, Song W. Cooperative interaction of Ig(alpha) and Ig(beta) of the BCR regulates the kinetics and specificity of antigen targeting. Int Immunol. 2002 Oct;14(10):1179-91. PMID:12356683
  4. ↑ Fuentes-Panana EM, Bannish G, van der Voort D, King LB, Monroe JG. Ig alpha/Ig beta complexes generate signals for B cell development independent of selective plasma membrane compartmentalization. J Immunol. 2005 Feb 1;174(3):1245-52. PMID:15661879
  5. ↑ Radaev S, Zou Z, Tolar P, Nguyen K, Nguyen A, Krueger PD, Stutzman N, Pierce S, Sun PD. Structural and functional studies of Igalphabeta and its assembly with the B cell antigen receptor. Structure. 2010 Aug 11;18(8):934-43. PMID:20696394 doi:10.1016/j.str.2010.04.019

3khq, resolution 1.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=3khq&oldid=3069001"