Literature DB >> 15680588

A common sequence-associated physicochemical feature for proteins of beta-trefoil family.

Ruizhen Xu1, Yi Xiao.   

Abstract

Different amino acid sequences can fold into similar tertiary structures but the reasons for it are not very clear. It has been suggested in the literature that these sequences may have some common features associated with them but the exact nature of such shared properties remains largely unknown. We studied a representative sample of proteins from the beta-trefoil family and observed that their amino acid sequences, despite being considerably divergent from each other, can be accounted for by matching to a repetition of three physicochemically similar segments. This observation in turn is consistent with the three-fold pseudo-symmetry in tertiary structures of these proteins.

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Year:  2005        PMID: 15680588     DOI: 10.1016/j.compbiolchem.2004.12.003

Source DB:  PubMed          Journal:  Comput Biol Chem        ISSN: 1476-9271            Impact factor:   2.877


  3 in total

1.  Identification and characterization of RbmA, a novel protein required for the development of rugose colony morphology and biofilm structure in Vibrio cholerae.

Authors:  Jiunn C N Fong; Kevin Karplus; Gary K Schoolnik; Fitnat H Yildiz
Journal:  J Bacteriol       Date:  2006-02       Impact factor: 3.490

2.  Symmetric key structural residues in symmetric proteins with beta-trefoil fold.

Authors:  Jianhui Feng; Mingfeng Li; Yanzhao Huang; Yi Xiao
Journal:  PLoS One       Date:  2010-11-30       Impact factor: 3.240

3.  How the Sequence of a Gene Specifies Structural Symmetry in Proteins.

Authors:  Xiaojuan Shen; Tongcheng Huang; Guanyu Wang; Guanglin Li
Journal:  PLoS One       Date:  2015-12-07       Impact factor: 3.240

  3 in total

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