Common features of the conformations of antigen-binding loops in immunoglobulins and application to modeling loop conformations.
Using database screening techniques we have examined the relationship between antigen-binding loops in immunoglobulins, and regions of similar conformation in other protein families. The conformations of most antigen-binding loops are not unique to immunoglobulins. But in many cases, the geometrical relationship between the loop and the peptides flanking it differs between the immunoglobulins and other structures with the same loop. We assess model building by data base screening, compared with that based on canonical structures.
Tramontano
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A
Istituto di Ricerche di Biologia Molecolare, Pomezia, Roma, Italy.
Lesk
A M
AM
D000595:Amino Acid Sequence; D000941:Antigens / Q000276:immunology; D001665:Binding Sites; D016208:Databases, Factual; D007136:Immunoglobulins / Q000737:chemistry* / Q000276:immunology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation
D000941:Antigens; D007136:Immunoglobulins