3MATRIX and 3MOTIF: a protein structure visualization system for conserved sequence motifs.
Computational methods such as sequence alignment and motif construction are useful in grouping related proteins into families, as well as helping to annotate new proteins of unknown function. These methods identify conserved amino acids in protein sequences, but cannot determine the specific functional or structural roles of conserved amino acids without additional study. In this work, we present 3MATRIX (http://3matrix.stanford.edu) and 3MOTIF (http://3motif.stanford.edu), a web-based sequence motif visualization system that displays sequence motif information in its appropriate three-dimensional (3D) context. This system is flexible in that users can enter sequences, keywords, structures or sequence motifs to generate visualizations. In 3MOTIF, users can search using discrete sequence motifs such as PROSITE patterns, eMOTIFs, or any other regular expression-like motif. Similarly, 3MATRIX accepts an eMATRIX position-specific scoring matrix, or will convert a multiple sequence alignment block into an eMATRIX for visualization. Each query motif is used to search the protein structure database for matches, in which the motif is then visually highlighted in three dimensions. Important properties of motifs such as sequence conservation and solvent accessible surface area are also displayed in the visualizations, using carefully chosen color shading schemes.
Bennett
Steven P
SP
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307, USA.
Lu
Lin
L
Brutlag
Douglas L
DL
D020816:Amino Acid Motifs; D000596:Amino Acids / Q000737:chemistry / Q000502:physiology; D000818:Animals; D003196:Computer Graphics; D017124:Conserved Sequence; D030562:Databases, Protein; D020407:Internet; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry; D016415:Sequence Alignment; D012984:Software
D000596:Amino Acids; D011506:Proteins