Haloacid dehalogenase-like hydrolase domain containing 2: Difference between revisions
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'''Haloacid dehalogenase-like hydrolase domain containing 2''' | |||
[[ | ===[[Report: Characterization of the 2HO4 protein using bioinformatics tools]]=== | ||
'''Abstract:''' Digging information about the functions of proteins whose structures have been determined by functional genomics can be a challenging task. However, once the bits and pieces have been collected from the various databases with biological information and the bioinformatics tools, it is possible to uncover the biological functions of such proteins. Using methods for structural, functional, and evolutionary analysis, we determined the possible function of the haloacid dehalogenase-like hydrolase domain containing 2, which may be refered to as 2HO4 (PDB code). 2HO4 is a member of the haloacid dehalogeanse (HAD) superfamily, and all members have three highly-conserved motifs. It presumably is a P-type ATPase involved in Mg2+ dependent phosphatase activity and is mainly expressed in the immune system and the CNS. Possible functions of 2HO4 may be to hydrolyze ATP and to transport ions across ion channels. Moreover, its sequence appears to be conserved amongst well studied animals, with the mouse version closest to the ancestral gene. The findings of this paper characterize some structural, functional, and evolutionary aspects of the haloacid dehalogenase-like hydrolase domain containing 2, but further research is warranted. | |||
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Latest revision as of 22:43, 11 June 2007
Haloacid dehalogenase-like hydrolase domain containing 2
Report: Characterization of the 2HO4 protein using bioinformatics tools
Abstract: Digging information about the functions of proteins whose structures have been determined by functional genomics can be a challenging task. However, once the bits and pieces have been collected from the various databases with biological information and the bioinformatics tools, it is possible to uncover the biological functions of such proteins. Using methods for structural, functional, and evolutionary analysis, we determined the possible function of the haloacid dehalogenase-like hydrolase domain containing 2, which may be refered to as 2HO4 (PDB code). 2HO4 is a member of the haloacid dehalogeanse (HAD) superfamily, and all members have three highly-conserved motifs. It presumably is a P-type ATPase involved in Mg2+ dependent phosphatase activity and is mainly expressed in the immune system and the CNS. Possible functions of 2HO4 may be to hydrolyze ATP and to transport ions across ion channels. Moreover, its sequence appears to be conserved amongst well studied animals, with the mouse version closest to the ancestral gene. The findings of this paper characterize some structural, functional, and evolutionary aspects of the haloacid dehalogenase-like hydrolase domain containing 2, but further research is warranted.
