Structural classification of CDR‐H3 in antibodies
1996; Wiley; Volume: 399; Issue: 1-2 Linguagem: Inglês
10.1016/s0014-5793(96)01252-5
ISSN1873-3468
AutoresHiroki Shirai, Akinori Kidera, Haruki Nakamura,
Tópico(s)Protein purification and stability
ResumoLarge varieties in the lengths and the amino acid sequences of the third complementarity determining region of the antibody heavy chain (CDR-H3) have made it difficult to establish a relationship between the sequences and the tertiary structures, in contrast to the other CDRs, which are classified by their canonical structures. A total of 55 CDR-H3 segments from well determined crystal structures were analyzed, and we have derived several remarkable rules, which could partly govern the CDR-H3 conformation dependence on the sequence. Since the rules are physically reasonable, they are expected to be applicable to structural modeling and design of antibodies.
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