TOPOLOGY FINGERPRINT APPROACH TO THE INVERSE PROTEIN FOLDING PROBLEM
TOPOLOGY FINGERPRINT APPROACH TO THE INVERSE PROTEIN FOLDING PROBLEM
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DOI：
10.1016/0022-2836(92)90693-e
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发表时间：
1992-09-05
影响因子：
5.6
通讯作者：
SKOLNICK, J
中科院分区：
文献类型：
--
作者：
GODZIK, A;KOLINSKI, A;SKOLNICK, J
我们描述了迄今为止最普遍的解决方案的问题相匹配的球状蛋白质序列的适当的三维结构。根据接触图和残基的掩埋/暴露模式，通过蛋白质“结构指纹”文库提供用于测试序列的筛选模板。然后，格子蒙特卡罗算法验证或驳回所提出的折叠的稳定性。在具有弱或不相关序列的蛋白质之间，例如球蛋白和藻蓝蛋白，磷酸丙糖异构酶的八元α β折叠，甚至天青蛋白和免疫球蛋白之间的密切结构等效性之间的已知结构相似性的例子被发现。
We describe the most general solution to date of the problem of matching globular protein sequences to the appropriate three-dimensional structure. The screening template, against which sequences are tested, is provided by a protein “structural fingerprint” library based on the contact map and the buried/exposed pattern of residues. Then, a lattice Monte Carlo algorithm validates or dismisses the stability of the proposed fold. Examples of known structural similarities between proteins having weakly or unrelated sequences such as the globins and phycocyanins, the eight-member α β fold of triose phosphate isomerase and even a close structural equivalence between azurin and immunoglobulins are found.