α链突变改变的镰状细胞血红蛋白纤维结构

Sickle cell hemoglobin fiber structure altered by alpha-chain mutation.

作者信息

Crepeau R H, Edelstein S J, Szalay M, Benesch R E, Benesch R, Kwong S, Edalji R

出版信息

Proc Natl Acad Sci U S A. 1981 Mar;78(3):1406-10. doi: 10.1073/pnas.78.3.1406.

DOI:10.1073/pnas.78.3.1406

PMID:6940165

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC319139/

Abstract

Hybrid hemoglobin molecules prepared with beta chains from hemoglobin S (beta 6 Glu leads to Val) and alpha chains from hemoglobin Sealy (alpha 47 Asp leads to His) form fibers with a novel structure. In contrast to the typical fibers of hemoglobin S with an average diameter of 22 nm and a solid cross section composed of 10 outer filaments surrounding a 4-filament core, the fibers of the alpha Sealy2 beta S2 hybrid are much larger, with a mean diameter of 32 nm and a unique double-hollow arrangement of filaments. Sealy--S fibers can be described by a model in which the two pairs of filaments most readily lost from fibers of hemoglobin S are missing to form the hollow regions, with an additional sheath of filaments added to form the overall larger structure.

摘要

用血红蛋白S的β链（β6谷氨酸突变为缬氨酸）和血红蛋白西利的α链（α47天冬氨酸突变为组氨酸）制备的杂合血红蛋白分子形成了具有新型结构的纤维。与血红蛋白S的典型纤维不同，后者平均直径为22纳米，其实心横截面由围绕4根细丝核心的10根外部细丝组成，α西利2βS2杂合纤维要大得多，平均直径为32纳米，具有独特的双空心细丝排列。西利-S纤维可以用一个模型来描述，在这个模型中，血红蛋白S纤维中最容易丢失的两对细丝缺失以形成空心区域，并添加额外的细丝鞘以形成整体更大的结构。