2h3n

From Proteopedia

(Difference between revisions)

Revision as of 06:29, 27 June 2018

Crystal structure of a surrogate light chain (LAMBDA5 and VpreB) homodimer

Structural highlights

2h3n is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2h32
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/2h3n"

@@ Line 1: / Line 1: @@
 ==Crystal structure of a surrogate light chain (LAMBDA5 and VpreB) homodimer==
 <StructureSection load='2h3n' size='340' side='right' caption='[[2h3n]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2h32|2h32]]</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=2h3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h3n OCA], [http://pdbe.org/2h3n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h3n RCSB], [http://www.ebi.ac.uk/pdbsum/2h3n 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=2h3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h3n OCA], [http://pdbe.org/2h3n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h3n RCSB], [http://www.ebi.ac.uk/pdbsum/2h3n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2h3n 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/h3/2h3n_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h3/2h3n_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2h3n

From Proteopedia

Revision as of 06:29, 27 June 2018

Crystal structure of a surrogate light chain (LAMBDA5 and VpreB) homodimer

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox