Kabat E A, Padlan E A, Davies D R
Proc Natl Acad Sci U S A. 1975 Jul;72(7):2785-8. doi: 10.1073/pnas.72.7.2785.
A comparison of five constant region sequences of human and mouse k and lambda immunoglobulin chains has been undertaken in order to reveal sequence homologies and evolutionary relationships. Simultaneously, a comparison with the three-dimensional structure of one mouse k-chain (McPC 603) has suggested structural reasons why many of the residues are invariant or conserved along k versus lambda lines. There are a number of residues that have remained invariant despite exposed positions for reasons that do not apppear to be connected with the folding of the CL domain.
为了揭示序列同源性和进化关系，对人类和小鼠κ及λ免疫球蛋白链的五个恒定区序列进行了比较。同时，与一条小鼠κ链（McPC 603）的三维结构进行比较，提示了许多残基沿κ链与λ链方向不变或保守的结构原因。有许多残基尽管处于暴露位置却保持不变，其原因似乎与CL结构域的折叠无关。
