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首页> 外文期刊>Journal of Molecular Biology >Resonance assignment and three-dimensional structure determination of a human alpha-defensin, HNP-1, by solid-state NMR.
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Resonance assignment and three-dimensional structure determination of a human alpha-defensin, HNP-1, by solid-state NMR.

机译：通过固态NMR进行人类α-防御素HNP-1的共振分配和三维结构测定。

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摘要

Human alpha-defensins [human neutrophil peptides (HNPs)] are immune defense mini-proteins that act by disrupting microbial cell membranes. Elucidating the three-dimensional (3D) structures of HNPs in lipid membranes is important for understanding their mechanisms of action. Using solid-state NMR (SSNMR), we have determined the 3D structure of HNP-1 in a microcrystalline state outside the lipid membrane, which provides benchmarks for structure determination and comparison with the membrane-bound state. From a suite of two-dimensional and 3D magic-angle spinning experiments, (13)C and (15)N chemical shifts that yielded torsion angle constraints were obtained, while inter-residue distances were obtained to restrain the 3D fold. Together, these constraints led to the first high-resolution SSNMR structure of a human defensin. The SSNMR structure has close similarity to the crystal structures of the HNP family, with the exception of the loop region between the first and second beta-strands. The difference, which is partially validated by direct torsion angle measurements of selected loop residues, suggests possible conformational variation and flexibility of this segment of the protein, which may regulate HNP interaction with the phospholipid membrane of microbial cells.
机译：人α-防御素[人中性粒细胞肽（HNP）]是通过破坏微生物细胞膜发挥作用的免疫防御微型蛋白。阐明脂质膜中HNP的三维（3D）结构对于理解其作用机理非常重要。使用固态NMR（SSNMR），我们已经确定了脂膜外部处于微晶状态的HNP-1的3D结构，这为结构确定和与膜结合状态的比较提供了基准。从一组二维和3D魔角旋转实验中，获得了产生扭转角约束的（13）C和（15）N化学位移，同时获得了残基间距离来限制3D折叠。这些限制因素共同导致了人类防御素的第一个高分辨率SSNMR结构。 SSNMR结构与HNP家族的晶体结构非常相似，但第一和第二β链之间的环区除外。这种差异通过选定环残基的直接扭转角测量得到了部分验证，表明该蛋白片段的可能构象变化和柔韧性，可能调节了HNP与微生物细胞磷脂膜的相互作用。

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