Crystal structure of human immunoglobulin fragment Fab new refined at 2.0 Å esolution
Crystal structure of human immunoglobulin fragment Fab new refined at 2.0 Å esolution
复制标题
人免疫球蛋白片段 Fab 的晶体结构在 2.0 Å 解析度下全新精制
DOI：
10.1002/prot.340140305
复制
发表时间：
1992
期刊：
影响因子：
--
通讯作者：
R. Poljak
中科院分区：
文献类型：
--
作者：
F. Saul;R. Poljak
人免疫球蛋白片段Fab New（IgG1，λ）的三维结构已精确到16.9%至20%分辨率的晶体学R因子。最终模型与理想几何结构的均方根偏差为键距0.014 μ m，键角3.03°。改进是基于一个新的X射线数据集，包括28，301个反射，F>2.5σ（F），分辨率为6.0至2.0 μ m。本文报道的精修程序的起始模型来自Brookhaven蛋白质数据库条目3FAB（1981年修订版）。初始模型和最终模型之间的差异包括VH的第三互补决定区（CDR 3）和第三框架区（FR 3）中以及CL和CH 1的一些暴露环中的修饰的多肽链折叠。通过观察差异电子密度图，确定了许多位置的氨基酸序列变化。氨基酸序列改变的掺入导致单克隆抗体“人源化”的改进的VH框架模型。
The three‐dimensional structure of the human immunoglobulin fragment Fab New (IgG1,λ) has been refined to a crystal‐lographic R‐factor of 16.9% to 2Å resolution. Rms deviations of the final model from ideal geometry are 0.014 Å for bond distances and 3.03° for bond angles. Refinement was based on a new X‐ray data set including 28,301 reflections with F>2.5σ(F) from 6.0 to 2.0 Å resolution. The starting model for the refinement procedure reported here is from the Brookhaven Protein Data Bank entry 3FAB (rev. 1981). Differences between the initial and final models include modified polypeptide‐chain folding in the third complementarity‐determining region (CDR3) and the third framework region (FR3) of VH and in some exposed loops of CL and CHl. Amino acid sequencechanges were determined at a number of positions by inspection of difference electron density maps. The incorporation of amino acid sequence changes results inan improved VH framework model for the “humanization” of monoclonal antibodies.
免疫球蛋白可变域的新排列：lambda 链二聚体 Bence-Jones 蛋白 Loc 的 X 射线晶体学分析。
影响因子：
2.9
作者：
Chang,CH;Short,MT;Westholm,FA;Stevens,FJ;Wang,BC;FureyJr,W;Solomon,A;Schiffer,M
通讯作者：
Schiffer,M