Cao Lihuan, Yan Xiaomei, Borysenko Christopher W, Blair Harry C, Wu Chaoqun, Yu Long
State Key Laboratory of Genetic Engineering, Institute of Genetics, Fudan University, Shanghai 200433, PR China.
FEMS Microbiol Lett. 2005 Oct 15;251(2):203-9. doi: 10.1016/j.femsle.2005.08.004.
We identified a cadherin-like domain (CHDL) using computational analysis. The CHDL domain is mostly distributed in Proteobacteria and Cyanobacteria, although it is also found in some eukaryotic proteins. Prediction of three-dimensional protein folding indicated that the CHDL domain has an immunoglobulin beta-sandwich fold and belongs to the cadherin superfamily. The CHDL domain does not have LDRE and DxNDN motifs, which are conserved in the cadherin domain, but has three other motifs: PxAxxD, DxDxD and YT-V/I-S/T-D, which might contribute to forming a calcium-binding site. The identification of this cadherin-like domain indicates that the cadherin superfamily may exhibit wider sequence and structural diversity than previously appreciated. Domain architecture analysis revealed that the CHDL domain is also associated with other adhesion domains as well as enzyme domains. Based on computational analysis and previous experimental data, we predict that the CHDL domain has calcium-binding and also carbohydrate-binding activity.
我们通过计算分析鉴定出一个类钙黏蛋白结构域(CHDL)。CHDL结构域主要分布在变形菌门和蓝细菌中,不过在一些真核生物蛋白质中也有发现。蛋白质三维折叠预测表明,CHDL结构域具有免疫球蛋白β-三明治折叠,属于钙黏蛋白超家族。CHDL结构域没有在钙黏蛋白结构域中保守的LDRE和DxNDN基序,但有其他三个基序:PxAxxD、DxDxD和YT-V/I-S/T-D,这些基序可能有助于形成钙结合位点。这个类钙黏蛋白结构域的鉴定表明,钙黏蛋白超家族可能表现出比以前认识到的更广泛的序列和结构多样性。结构域架构分析显示,CHDL结构域还与其他黏附结构域以及酶结构域相关。基于计算分析和先前的实验数据,我们预测CHDL结构域具有钙结合以及碳水化合物结合活性。