2h3n: Difference between revisions
New page: left|200px<br /> <applet load="2h3n" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h3n, resolution 2.3Å" /> '''Crystal structure of... |
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[[Image:2h3n. | [[Image:2h3n.jpg|left|200px]]<br /><applet load="2h3n" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="2h3n, resolution 2.3Å" /> | caption="2h3n, resolution 2.3Å" /> | ||
'''Crystal structure of a surrogate light chain (LAMBDA5 and VpreB) homodimer'''<br /> | '''Crystal structure of a surrogate light chain (LAMBDA5 and VpreB) homodimer'''<br /> | ||
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==Overview== | ==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. | 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== | ==About this Structure== | ||
2H3N is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 2H3N is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H3N OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: v- and c-type immunoglobulin fold]] | [[Category: v- and c-type immunoglobulin fold]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:14:43 2008'' | ||
Revision as of 13:14, 23 January 2008
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Crystal structure of a surrogate light chain (LAMBDA5 and VpreB) homodimer
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
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
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