通过质子磁共振鉴定小鼠表皮生长因子溶液结构中的两种反平行β-折叠构象。
Identification of two anti-parallel beta-sheet conformations in the solution structure of murine epidermal growth factor by proton magnetic resonance.
作者信息
Montelione G T, Wüthrich K, Nice E C, Burgess A W, Scheraga H A
出版信息
Proc Natl Acad Sci U S A. 1986 Nov;83(22):8594-8. doi: 10.1073/pnas.83.22.8594.
Abstract
Epidermal growth factor (EGF) is a small mitogenic protein. Proteins with sequence homology with EGF or with its membrane-bound protein receptor have been proposed to play a role in oncogenesis. This report describes solution NMR data that provide evidence that the solution conformation of murine EGF includes an anti-parallel beta-sheet structure involving residues S2-P4, V19-I23, and S28-N32; a small anti-parallel beta-sheet involving residues Y37-S38 and T44-R45; and a multiple-bend (or short irregular helix) structure for residues C6-C14 that is disulfide bonded to the V19-I23/S28-N32 beta-sheet. Implications of these results for structure and function studies of EGF and for molecular design of EGF and homologous alpha-type transforming growth factors are discussed.
摘要
表皮生长因子（EGF）是一种小的促有丝分裂蛋白。与EGF或其膜结合蛋白受体具有序列同源性的蛋白质被认为在肿瘤发生中起作用。本报告描述了溶液核磁共振数据，这些数据提供了证据表明小鼠EGF的溶液构象包括一个反平行β-折叠结构，涉及残基S2-P4、V19-I23和S28-N32；一个涉及残基Y37-S38和T44-R45的小反平行β-折叠；以及残基C6-C14的多弯曲（或短不规则螺旋）结构，该结构通过二硫键与V19-I23/S28-N32β-折叠相连。讨论了这些结果对EGF结构和功能研究以及EGF和同源α型转化生长因子分子设计的意义。
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