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Computational Biology Study of S100 Family with Suggestions for Crystallization

Computational Biology Study of S100 Family with Suggestions for Crystallization
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摘要 The S100 family is a class of calcium regulated proteins with EF hand. They are widely distributed and are implicated in diverse intracellular and extracellular physiological processes. A study of the S100 family using computational biology methods such as multiple sequence alignment, structural alignment and the construction of an evolutionary tree will promote understanding of S100 protein structures and their function, and could provide suggestions for crystallization. The S100 family is a class of calcium regulated proteins with EF hand. They are widely distributed and are implicated in diverse intracellular and extracellular physiological processes. A study of the S100 family using computational biology methods such as multiple sequence alignment, structural alignment and the construction of an evolutionary tree will promote understanding of S100 protein structures and their function, and could provide suggestions for crystallization.
出处 《Tsinghua Science and Technology》 SCIE EI CAS 2001年第3期248-252,共5页 清华大学学报(自然科学版(英文版)
基金 the National Natural Science Foundationof China(No.39870 174and39970 15 5 ) Project"86 3"(10 3130 30 6 ) Project " 973" (G199990 75 6 0 2 G19990 1190 2and19980 5 110 5 )
关键词 S100 family computational biology sequence alignment structural alignment CRYSTALLIZATION S100 family computational biology sequence alignment structural alignment crystallization
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参考文献4

  • 1Thompsan J D,Higgins D G,Gibson T J.Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting,positions-specific gap penalties and weight matrix choice[].Nucleic Acids Research.1994
  • 2Fiona E M Gibbs,Mark C Wilkinson,Philip S Rudland,et al.Interactions in vitro ofp9Ka, the rat S-100-related, metastasis-inducing, calcium-binding protein[].Journal of Biological Chemistry.1994
  • 3Brodersen D E,Nyborg J,Kjeldgaard M.Zincbinding site of an S100 protein revealed.Two crystal structures of Ca2+ -bound human psoriasin (S100A7)in the Zn2+ -loaded and Zn2+ -free states[].Biochemistry.1999
  • 4Bryony H Lloyd,Angela Platt -Higgins,Philip S Rudland,et al.Human S100A4 ( p9ka ) induces the metastatic phenotype upon benign tumour cells[].Oncegene.1998

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