Kornev Alexandr P, Taylor Susan S, Ten Eyck Lynn F
Howard Hughes Medical Institute, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.
Proc Natl Acad Sci U S A. 2008 Sep 23;105(38):14377-82. doi: 10.1073/pnas.0807988105. Epub 2008 Sep 11.
Structures of set of serine-threonine and tyrosine kinases were investigated by the recently developed bioinformatics tool Local Spatial Patterns (LSP) alignment. We report a set of conserved motifs comprised mostly of hydrophobic residues. These residues are scattered throughout the protein sequence and thus were not previously detected by traditional methods. These motifs traverse the conserved protein kinase core and play integrating and regulatory roles. They are anchored to the F-helix, which acts as an organizing "hub" providing precise positioning of the key catalytic and regulatory elements. Consideration of these discovered structures helps to explain previously inexplicable results.
通过最近开发的生物信息学工具局部空间模式（LSP）比对，研究了丝氨酸 - 苏氨酸激酶和酪氨酸激酶组的结构。我们报告了一组主要由疏水残基组成的保守基序。这些残基散布在整个蛋白质序列中，因此以前传统方法未检测到。这些基序贯穿保守的蛋白激酶核心并发挥整合和调节作用。它们锚定在F螺旋上，F螺旋充当组织“中心”，为关键的催化和调节元件提供精确定位。对这些发现结构的考虑有助于解释以前无法解释的结果。
