2h3n: Difference between revisions

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[[Image:2h3n.jpg|left|200px]]
{{Seed}}
[[Image:2h3n.png|left|200px]]


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{{STRUCTURE_2h3n|  PDB=2h3n  |  SCENE=  }}  
{{STRUCTURE_2h3n|  PDB=2h3n  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_17431183}}


==About this Structure==
==About this Structure==
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[[Category: Beta sheet]]
[[Category: Beta sheet]]
[[Category: V- and c-type immunoglobulin fold]]
[[Category: V- and c-type immunoglobulin fold]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:49:46 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:26:14 2008''

Revision as of 20:26, 28 July 2008

File:2h3n.png

Template:STRUCTURE 2h3n

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

Template:ABSTRACT PUBMED 17431183

About this Structure

2H3N 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 Mon Jul 28 23:26:14 2008

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