1rjc: Difference between revisions

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[[Image:1rjc.gif|left|200px]]
{{Seed}}
[[Image:1rjc.png|left|200px]]


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{{STRUCTURE_1rjc|  PDB=1rjc  |  SCENE=  }}  
{{STRUCTURE_1rjc|  PDB=1rjc  |  SCENE=  }}  


'''Crystal structure of the camelid single domain antibody cAb-Lys2 in complex with hen egg white lysozyme'''
===Crystal structure of the camelid single domain antibody cAb-Lys2 in complex with hen egg white lysozyme===




==Overview==
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A central paradigm in immunology states that successful generation of high affinity antibodies necessitates an immense primary repertoire of antigen-combining sites. Much of the diversity of this repertoire is provided by varying one antigen binding loop, created by inserting randomly a D (diversity) gene out of a small pool between the V and J genes. It is therefore assumed that any particular D-encoded region surrounded by different V and J regions adopts a different conformation. We have solved the structure of two lysozyme-specific variable domains of heavy-chain antibodies isolated from two strictly unrelated dromedaries. These antibodies recombined identical D gene sequences to different V and J precursors with significant variance in their V(D)J junctions. Despite these large differences, the D-encoded loop segments adopt remarkably identical architectures, thus directing the antibodies toward identical epitopes. Furthermore, a striking convergent maturation process occurred in the V region, adapting both binders for their sub-nanomolar affinity association with lysozyme. Hence, on a structural level, humoral immunity may rely more on well developed maturation and selection systems than on the acquisition of large primary repertoires.
The line below this paragraph, {{ABSTRACT_PUBMED_15659390}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_15659390}}


==About this Structure==
==About this Structure==
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[[Category: Immunoglobulin fold]]
[[Category: Immunoglobulin fold]]
[[Category: Protein-protein hetero complex]]
[[Category: Protein-protein hetero complex]]
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