2h32: Difference between revisions
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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.]] | ||
[[Category: | [[Category: Beta sheet]] | ||
[[Category: | [[Category: V and c-type ig fold]] | ||
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Revision as of 02:48, 4 May 2008
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