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Journal of Bioinformatics and Computational Biology

Publication date: 2013-02-01
Volume: 11 Pages: 1340008 -
Publisher: Imperial College Press

Author:

Maurer-Stroh, Sebastian
Gao, He ; Han, Hao ; Baeten, Liesbeth ; Schymkowitz, Joost ; Rousseau, Frederic ; Zhang, Louxin ; Eisenhaber, Frank

Keywords:

Science & Technology, Life Sciences & Biomedicine, Technology, Biochemical Research Methods, Computer Science, Interdisciplinary Applications, Mathematical & Computational Biology, Biochemistry & Molecular Biology, Computer Science, Datamining, protein structure database, protein structural motif, zinc binding, zinc finger, HMM, protein sequence motifs, SITES, Amino Acid Sequence, Carrier Proteins, Computer Simulation, Data Mining, Databases, Protein, Models, Chemical, Models, Molecular, Molecular Sequence Data, Protein Conformation, Sequence Analysis, Protein, 0601 Biochemistry and Cell Biology, 0801 Artificial Intelligence and Image Processing, Bioinformatics, 3102 Bioinformatics and computational biology, 4601 Applied computing

Abstract:

Data mining in protein databases, derivatives from more fundamental protein 3D structure and sequence databases, has considerable unearthed potential for the discovery of sequence motif-structural motif-function relationships as the finding of the U-shape (Huf-Zinc) motif, originally a small student's project, exemplifies. The metal ion zinc is critically involved in universal biological processes, ranging from protein-DNA complexes and transcription regulation to enzymatic catalysis and metabolic pathways. Proteins have evolved a series of motifs to specifically recognize and bind zinc ions. Many of these, so called zinc fingers, are structurally independent globular domains with discontinuous binding motifs made up of residues mostly far apart in sequence. Through a systematic approach starting from the BRIX structure fragment database, we discovered that there exists another predictable subset of zinc-binding motifs that not only have a conserved continuous sequence pattern but also share a characteristic local conformation, despite being included in totally different overall folds. While this does not allow general prediction of all Zn binding motifs, a HMM-based web server, Huf-Zinc, is available for prediction of these novel, as well as conventional, zinc finger motifs in protein sequences. The Huf-Zinc webserver can be freely accessed through this URL ( http://mendel.bii.a-star.edu.sg/METHODS/hufzinc/ ).