期刊
STRUCTURE
卷 22, 期 1, 页码 22-34出版社
CELL PRESS
DOI: 10.1016/j.str.2013.10.006
关键词
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资金
- National Science Council [NSC 100IDP006-3, NSC 99-2311-B-001-014-MY3]
- Genomics Research Center at Academia Sinica [AS-100-TP2-B01]
Protein structural stability and biological functionality are dictated by the formation of intradomain cores and interdomain interfaces, but the intricate sequence-structure-function interrelationships in the packing of protein cores and interfaces remain difficult to elucidate due to the intractability of enumerating all packing possibilities and assessing the consequences of all the variations. In this work, groups of beta strand residues of model antibody variable domains were randomized with saturated mutagenesis and the functional variants were selected for high-throughput sequencing and high-throughput thermal stability measurements. The results show that the sequence preferences of the intradomain hydrophobic core residues are strikingly flexible among hydrophobic residues, implying that these residues are coupled indirectly with antigen binding through energetic stabilization of the protein structures. By contrast, the interdomain interface residues are directly coupled with antigen binding. The interdomain interlace should be treated as an integral part of the antigen-binding site.
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