Prelli F, Frangione B
Department of Pathology, New York University Medical Center, NY 10016.
J Immunol. 1992 Feb 1;148(3):949-52.
The complete sequence of a gamma 2-H chain disease protein BUR is presented. This mutant, a dimer of a 348-residue chain, linked by four disulfide bridges, is composed of a complete V region, hinge, CH2, and CH3 domains. There is one deletion, the CH1 domain, which includes the cysteine residue bridging the H to L chain. Although the V region is encoded by the VHI and JHIII genes, it has several distinctions: methionine at position 11, two unique cysteine residues in the second complementarity determining region (CDR2), and three glycosylation sites, two of which are located in the CDR2 and CDR3 regions. These distinctive characteristics of BUR VH within the framework of a normal VHI may be affected by extensive somatic mutation or by a rare and previously unanalyzed VH gene.
本文展示了γ2-H链病蛋白BUR的完整序列。该突变体是由一条348个残基的链通过四个二硫键连接而成的二聚体，由完整的V区、铰链区、CH2和CH3结构域组成。存在一个缺失，即CH1结构域，其包括连接重链和轻链的半胱氨酸残基。虽然V区由VHI和JHIII基因编码，但它有几个不同之处：第11位为甲硫氨酸，在第二个互补决定区（CDR2）有两个独特的半胱氨酸残基，以及三个糖基化位点，其中两个位于CDR2和CDR3区域。在正常VHI框架内BUR VH的这些独特特征可能受到广泛的体细胞突变或一个罕见且以前未分析过的VH基因的影响。
