2h32: Difference between revisions

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New page: left|200px<br /> <applet load="2h32" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h32, resolution 2.70Å" /> '''Crystal structure o...
 
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[[Image:2h32.gif|left|200px]]<br />
[[Image:2h32.jpg|left|200px]]<br /><applet load="2h32" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2h32" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2h32, resolution 2.70&Aring;" />
caption="2h32, resolution 2.70&Aring;" />
'''Crystal structure of the pre-B cell receptor'''<br />
'''Crystal structure of the pre-B cell receptor'''<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.
==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==
2H32 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2H32 OCA].  
2H32 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H32 OCA].  


==Reference==
==Reference==
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[[Category: v and c-type ig folds]]
[[Category: v and c-type ig folds]]


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