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HIV-1 GP41 TERTIARY STRUCTURE STUDIED BY EPR SPECTROSCOPY

机译：EPR光谱法研究HIV-1 GP41的三级结构

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HIV gp41 is the transmembrane glycoprotein responsible for fusion of viral and cellular membranes, enabling viral entry. The structure of gp41 was studied using two synthetic peptides derived from the ectodomain of gp41: a 38-residue peptide from the ''heptad repeat'' region (hr.wt), and a 34-residue peptide from a region closer to the C-terminus (bt.wt). These peptides were found to form a trimer of heterodimers with approximately 80% alpha-helicity. To study their alignment, distances between spin-labels attached to Cys residues on Cys-substituted peptides were measured using a recently-developed electron paramagnetic resonance method [Rabenstein, M. D., & Shin, Y.-K. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 8239-8243]. The heterotrimeric peptides were found to be antiparallel, consistent with a study on proteolytically cleaved peptide fragments of, gp41 [Lu, M., Blacklow, S. C., & Kim, P. S. (1995) Nat. Struct. Biol. 2, 1075-1082], Furthermore, the C-terminal 19 residues of hr.wt are not apposed to bt.wt, and 15 residues of bt.wt extend beyond the end of hr.wt. Consistent with this: alignment are tertiary interactions between specific sires of these peptides probed by spin-label mobility. Additionally, a second pair of peptides was studied. From the model, these are expected to align with complete overlap. Alone, neither was helical, but when mixed. they were 83% helical. Based on the alignment of the peptides, a model of the prefusogenic form of gp41 was constructed which is significantly different from the structure of influenza hemagglutinin.
机译：HIV gp41是跨膜糖蛋白，负责病毒和细胞膜的融合，使病毒进入。使用两个衍生自gp41胞外域的合成肽研究了gp41的结构：一个来自``heptad repeat''区域（hr.wt）的38个残基的肽段，另一个是来自距离C较近的区域的34个残基的肽段。 -总站（bt.wt）。发现这些肽形成具有约80％的α-螺旋度的异二聚体的三聚体。为了研究它们的比对，使用最近开发的电子顺磁共振法[Rabenstein，M.D。，＆Shin，Y.-K。]测量了与Cys-取代的肽上的Cys残基连接的自旋标记之间的距离。 （1995）美国国家科学院院刊。 Natl。学院科学U.S.A. 92，8239-8243]。发现异三聚体肽是反平行的，与对gp41的蛋白水解切割的肽片段的研究一致[Lu，M.，Blacklow，S.C。，和Kim，P.S。（1995）Nat.Natl.Acad.Sci.USA，89：3587-5877]。结构。生物学2，1075-1082]，此外，hr.wt的C末端19个残基未与bt.wt相连，而bt.wt的15个残基延伸至hr.wt的末端之外。与此一致：比对是通过自旋标记迁移率探测的这些肽的特定序列之间的三级相互作用。另外，研究了第二对肽。从模型中，可以期望它们完全重叠。一个人，既不是螺旋形的，而是混合在一起的。他们是83％的螺旋。基于肽的比对，构建了与流感血凝素的结构显着不同的gp41的前融合形式的模型。

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