免疫球蛋白κ链恒定区的多字母氨基酸序列比较。
Multiple-alphabet amino acid sequence comparisons of the immunoglobulin kappa-chain constant domain.
作者信息
Karlin S, Ghandour G
出版信息
Proc Natl Acad Sci U S A. 1985 Dec;82(24):8597-601. doi: 10.1073/pnas.82.24.8597.
Abstract
We compare the amino acid sequences of the constant domains of the immunoglobulin kappa chain of human, mouse, and rabbit by using four classification schemes ("alphabets") of the 20 amino acids based on their chemical, functional, charge, and structural properties. The comparison reveals three regions of pronounced similarity across the three species, independent of allotype. Two of these regions (residues 65-73 and 99-103) entail a high degree of identity at the DNA level and are distinguished from the rest of the constant domain in codon usage and in the dinucleotide sequence at abutting sites of adjacent codons. Residues 22-29 are highly conserved among the three species in the chemical and functional alphabets but do not show any three-sequence significant amino acid block identities. These results are discussed in terms of transcript processing, effector functions, and structural interactions within the constant domain and with the heavy chain.
摘要
我们通过使用基于20种氨基酸的化学、功能、电荷和结构特性的四种分类方案（“字母表”），比较了人、小鼠和兔免疫球蛋白κ链恒定区的氨基酸序列。比较结果显示，在这三个物种中存在三个明显相似的区域，与同种异型无关。其中两个区域（第65 - 73位和第99 - 103位残基）在DNA水平上具有高度同一性，并且在密码子使用以及相邻密码子邻接位点的二核苷酸序列方面与恒定区的其余部分有所不同。在化学和功能字母表中，第22 - 29位残基在这三个物种中高度保守，但未显示出任何三联体显著氨基酸块同一性。我们从转录本加工、效应功能以及恒定区内和与重链的结构相互作用等方面讨论了这些结果。
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