Abstract

Natural resistance associated macrophage protein 2 plays an important role in adsorption of a broad range of divalent metal ions, including iron, cobalt, zinc, copper, nickel, manganese, cadmium and lead. The protein contains 12 putative transmembrane domains, two highly conserved and mutation sensitive histidines were found in the predicted transmembrane domain 6, mutation of two histidines at either or both sites causing deficiency of function. In this paper, the structure of the peptide from transmembrane 6 of natural resistance associated macrophage protein 2 was investigated in 60% hexafluoroisopropanol aqueous solution by circular dichroism and nuclear magnetic resonance spectroscopy. Our study demonstrated the peptide forms a discontinuous α helix structure with two helices spanning over Ala256-Ile259 and Asn268-Ser278.

摘要

天然抗性相关的巨噬细胞蛋白2在吸附多种二价金属离子（包括铁，钴，锌，铜，镍，锰，镉和铅）中起重要作用。该蛋白质包含12个推定的跨膜结构域，在预测的跨膜结构域6中发现了两个高度保守且对突变敏感的组氨酸，这两个组氨酸在一个或两个位点的突变导致功能缺失。本文利用圆二色性和核磁共振波谱研究了天然抗性巨噬细胞蛋白2跨膜6肽的结构，该结构是在60％六氟异丙醇水溶液中进行的。我们的研究表明，该肽形成了不连续的α螺旋结构，其中两个螺旋跨越Ala256-Ile259和Asn268-Ser278。