Godzik A, Kolinski A, Skolnick J
Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.
J Mol Biol. 1992 Sep 5;227(1):227-38. doi: 10.1016/0022-2836(92)90693-e.
We describe the most general solution to date of the problem of matching globular protein sequences to the appropriate three-dimensional structures. 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 alpha/beta fold of triose phosphate isomerase and even a close structural equivalence between azurin and immunoglobulins are found.
我们描述了迄今为止将球状蛋白质序列与合适的三维结构进行匹配问题的最通用解决方案。用于测试序列的筛选模板由基于接触图和残基掩埋/暴露模式的蛋白质“结构指纹”库提供。然后，一种晶格蒙特卡罗算法验证或排除所提出折叠结构的稳定性。发现了具有弱相关或不相关序列的蛋白质之间已知结构相似性的例子，例如球蛋白和藻蓝蛋白、磷酸丙糖异构酶的八元α/β折叠，甚至连蓝铜蛋白和免疫球蛋白之间也存在紧密的结构等效性。
