CHDL: A cadherin-like domain in Proteobacteria and Cyanobacteria

被引:25
作者
Cao, LH
Yan, XM
Borysenko, CW
Blair, HC
Wu, CQ
Yu, L [1 ]
机构
[1] Fudan Univ, Inst Genet, State Key Lab Genet Engn, Shanghai 200433, Peoples R China
[2] Carnegie Mellon Univ, Mellon Coll Sci, Pittsburgh, PA 15213 USA
[3] Univ Pittsburgh, Dept Pathol, Pittsburgh, PA 15261 USA
[4] Vet Affairs Hlth Syst, Pittsburgh, PA 15261 USA
关键词
calcium-binding proteins; cadherin superfamily; carbohydrate binding proteins;
D O I
10.1016/j.femsle.2005.08.004
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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 superfarnhy 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. (C) 2005 Published by Elsevier B.V. on behalf of the Federation of European Microbiological Societies.
引用
收藏
页码:203 / 209
页数:7
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