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2h32

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Revision as of 06:22, 27 June 2018

Crystal structure of the pre-B cell receptor

Structural highlights

2h32 is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	VPREB1, VPREB (HUMAN), IGLL1, IGL1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[IGLL1_HUMAN] Defects in IGLL1 are the cause of agammaglobulinemia type 2 (AGM2) [MIM:613500]. It is a primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B-cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life.

Function

[VPREB_HUMAN] Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells. This complex presumably regulates Ig gene rearrangements in the early steps of B-cell differentiation. [IGLL1_HUMAN] Critical for B-cell development.^[1]

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 pre-B cell receptor (pre-BCR) serves as a checkpoint in B cell development. In the 2.7 angstrom structure of a human pre-BCR Fab-like fragment, consisting of an antibody heavy chain (HC) paired with the surrogate light chain, the "unique regions" of VpreB and lambda5 replace the complementarity-determining region 3 (CDR3) loop of an antibody light chain and appear to "probe" the HC CDR3, potentially influencing the selection of the antibody repertoire. Biochemical analysis indicates that the pre-BCR is impaired in its ability to recognize antigen, which, together with electron microscopic visualization of a pre-BCR dimer, suggests ligand-independent oligomerization as the likely signaling mechanism.

Structural insight into pre-B cell receptor function.,Bankovich AJ, Raunser S, Juo ZS, Walz T, Davis MM, Garcia KC Science. 2007 Apr 13;316(5822):291-4. PMID:17431183^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Minegishi Y, Coustan-Smith E, Wang YH, Cooper MD, Campana D, Conley ME. Mutations in the human lambda5/14.1 gene result in B cell deficiency and agammaglobulinemia. J Exp Med. 1998 Jan 5;187(1):71-7. PMID:9419212
↑ Bankovich AJ, Raunser S, Juo ZS, Walz T, Davis MM, Garcia KC. Structural insight into pre-B cell receptor function. Science. 2007 Apr 13;316(5822):291-4. PMID:17431183 doi:http://dx.doi.org/316/5822/291

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2h32"

Categories: Human | Bankovich, A J | Beta sheet | Immune system | V and c-type ig fold

@@ Line 1: / Line 1: @@
 ==Crystal structure of the pre-B cell receptor==
 <StructureSection load='2h32' size='340' side='right' caption='[[2h32]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VPREB1, VPREB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), IGLL1, IGL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2h32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h32 OCA], [http://pdbe.org/2h32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h32 RCSB], [http://www.ebi.ac.uk/pdbsum/2h32 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=2h32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h32 OCA], [http://pdbe.org/2h32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h32 RCSB], [http://www.ebi.ac.uk/pdbsum/2h32 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2h32 ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h3/2h32_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h3/2h32_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2h32 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

2h32

From Proteopedia

Revision as of 06:22, 27 June 2018

Crystal structure of the pre-B cell receptor

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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