2h32

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[[Image:2h32.jpg|left|200px]]
[[Image:2h32.jpg|left|200px]]
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{{Structure
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|PDB= 2h32 |SIZE=350|CAPTION= <scene name='initialview01'>2h32</scene>, resolution 2.70&Aring;
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The line below this paragraph, containing "STRUCTURE_2h32", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE= VPREB1, VPREB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), IGLL1, IGL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_2h32| PDB=2h32 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/2h32 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h32 RCSB]</span>
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'''Crystal structure of the pre-B cell receptor'''
'''Crystal structure of the pre-B cell receptor'''
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Bankovich, A J.]]
[[Category: Bankovich, A J.]]
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[[Category: beta sheet]]
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[[Category: Beta sheet]]
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[[Category: v and c-type ig fold]]
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[[Category: V and c-type ig fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:48:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:24:46 2008''
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Revision as of 02:48, 4 May 2008

Image:2h32.jpg

Template:STRUCTURE 2h32

Crystal structure of the pre-B cell receptor


Overview

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.

About this Structure

2H32 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 05:48:37 2008

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