TOPOLOGICAL DISTRIBUTION OF 4-ALPHA-HELIX BUNDLES
TOPOLOGICAL DISTRIBUTION OF 4-ALPHA-HELIX BUNDLES
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DOI：
10.1073/pnas.86.17.6592
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发表时间：
1989-09-01
影响因子：
11.1
通讯作者：
COHEN, FE
中科院分区：
文献类型：
--
作者：
PRESNELL, SR;COHEN, FE
四个-α-螺旋束是球状蛋白质中常见的结构基序，它为蛋白质骨架拓扑结构的预测约束提供了一个很好的研究平台。对Brookhaven晶体蛋白质数据库和其它文献来源的详尽检查导致发现了20个推定的四-α-螺旋束应用的分析方法，检查之间的差异，溶剂可接触的表面积在包装和部分未包装的束减少了结构的数量为16。Angular需求进一步将捆绑包列表减少到13个。在这些束中的12个中，所有相邻螺旋对都以反平行方式取向。如果螺旋宏观偶极效应对天然结构的稳定性做出实质性贡献，则该分布与预期的结构类型一致。在这项研究中的特点和分类提示结构预测工作中使用的约束条件的重新评估。
The four-.alpha.-helix bundle, a common structural motif in globular proteins, provides an excellent forum for the examination of predictive constraints for protein backbone topology. An exhaustive examination of the Brookhaven Crystallographic Protein Data Bank and other literature sources has lead to the discovery of 20 putative four-.alpha.-helix bundles. Application of an analytical method that examines the difference between solvent-accessible surface areas in packed and partially unpacked bundles reduced the number of structures to 16. Angular requirements further reduced the list of bundles to 13. In 12 of these bundles, all pairs of neighboring helices were oriented in an anti-parallel fashion. This distribution is in accordance with structure types expected if the helix macro dipole effect makes a substantial contribution to the stability of the native structure. The characterizations and classifications made in this study prompt a reevaluation of constraints used in structure prediction efforts.