2h32
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | The pre-B cell receptor (pre-BCR) serves as a checkpoint in B cell | + | 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. |
| + | |||
| + | ==Disease== | ||
| + | Known diseases associated with this structure: Agammaglobulinemia, autosomal recessive OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=146770 146770]] | ||
==About this Structure== | ==About this Structure== | ||
| Line 13: | Line 16: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Bankovich, A | + | [[Category: Bankovich, A J.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: beta sheets]] | [[Category: beta sheets]] | ||
[[Category: v and c-type ig folds]] | [[Category: v and c-type ig folds]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:37:42 2008'' |
Revision as of 15:37, 21 February 2008
|
Crystal structure of the pre-B cell receptor
Contents |
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.
Disease
Known diseases associated with this structure: Agammaglobulinemia, autosomal recessive OMIM:[146770]
About this Structure
2H32 is a Protein complex structure of sequences from Homo sapiens with as ligand. 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 Thu Feb 21 17:37:42 2008
