This component of the program project provides informatics support and analysis. In the next phase, focusing on the structural impact of alternative splicing, there are five principle goals: First, development of a database that integrates a wide range of information relevant to alternative splicing in higher eukaryotes, particularly human, so that the most interesting and rewarding cases can be selected for experimental study. The design of the database is based on our experience with integrating information for target choice in the present phase of the project. Second, development of tools for automatically assessing the reliability of data indicating alternative splicing. At this stage of the development of the field, it is critical to be able to easily assess the data supporting a splice, before committing experimental effort. Third, production of structure models, allowing a visual appreciation of the likely impact of splicing on structure. Fourth, development of a comprehensive public database that will provide information on alternate splicing in a structural context, obtained from our own and work that of others, and using both models and experimental structures. This resource will allow users to obtain information about specific proteins, and to perform analyses on the general relationship between splicing, structure, function and disease. Fifth, the development and application of tools to analyze the relationship between splicing, structure and function. Tools for the analysis of function developed in the present phase will form the basis of these.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Program Projects (P01)
Project #
5P01GM057890-09
Application #
7553214
Study Section
Special Emphasis Panel (ZRG1)
Project Start
Project End
Budget Start
2006-08-01
Budget End
2007-07-31
Support Year
9
Fiscal Year
2006
Total Cost
$164,012
Indirect Cost
Name
University of MD Biotechnology Institute
Department
Type
DUNS #
603819210
City
Baltimore
State
MD
Country
United States
Zip Code
21202
Zhao, Hong; Lim, Kap; Choudry, Anthony et al. (2012) Correlation of structure and function in the human hotdog-fold enzyme hTHEM4. Biochemistry 51:6490-2
Chen, Chen; Gorlatova, Natalia; Kelman, Zvi et al. (2011) Structures of p63 DNA binding domain in complexes with half-site and with spacer-containing full response elements. Proc Natl Acad Sci U S A 108:6456-61
Lim, Kap; Pullalarevu, Sadhana; Surabian, Karen Talin et al. (2010) Structural basis for the mechanism and substrate specificity of glycocyamine kinase, a phosphagen kinase family member. Biochemistry 49:2031-41
Chen, Chen; Sun, Qihong; Narayanan, Buvaneswari et al. (2010) Structure of oxalacetate acetylhydrolase, a virulence factor of the chestnut blight fungus. J Biol Chem 285:26685-96
Melamud, Eugene; Moult, John (2009) Stochastic noise in splicing machinery. Nucleic Acids Res 37:4873-86
Melamud, Eugene; Moult, John (2009) Structural implication of splicing stochastics. Nucleic Acids Res 37:4862-72
Chao, Kinlin L; Lim, Kap; Lehmann, Christopher et al. (2008) The Escherichia coli YdcF binds S-adenosyl-L-methionine and adopts an alpha/beta-fold characteristic of nucleotide-utilizing enzymes. Proteins 72:506-9
Zhuang, Zhihao; Song, Feng; Zhao, Hong et al. (2008) Divergence of function in the hot dog fold enzyme superfamily: the bacterial thioesterase YciA. Biochemistry 47:2789-96
Willis, Mark A; Zhuang, Zhihao; Song, Feng et al. (2008) Structure of YciA from Haemophilus influenzae (HI0827), a hexameric broad specificity acyl-coenzyme A thioesterase. Biochemistry 47:2797-805
Sari, Nese; He, Yanan; Doseeva, Victoria et al. (2007) Solution structure of HI1506, a novel two-domain protein from Haemophilus influenzae. Protein Sci 16:977-82

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