MegaMotifBase: a database of structural motifs in protein families and superfamilies

Structural motifs are important for the integrity of a protein fold and can be employed to design and rationalize protein engineering and folding experiments. Such conserved segments represent the conserved core of a family or superfamily and can be crucial for the recognition of potential new members in sequence and structure databases. We present a database, MegaMotifBase, that compiles a set of important structural segments or motifs for protein structures. Motifs are recognized on the basis of both sequence conservation and preservation of important structural features such as amino acid preference, solvent accessibility, secondary structural content, hydrogen-bonding pattern and residue packing. This database provides 3D orientation patterns of the identified motifs in terms of inter-motif distances and torsion angles. Important applications of structural motifs are also provided in several crucial areas such as similar sequence and structure search, multiple sequence alignment and homology modeling. MegaMotifBase can be a useful resource to gain knowledge about structure and functional relationship of proteins. The database can be accessed from the URL http://caps.ncbs.res.in/MegaMotifbase/index.html

[1]  John P. Overington,et al.  A structural basis for sequence comparisons. An evaluation of scoring methodologies. , 1993, Journal of molecular biology.

[2]  Charlotte M. Deane,et al.  JOY: protein sequence-structure representation and analysis , 1998, Bioinform..

[3]  Ramanathan Sowdhamini,et al.  PASS2: an automated database of protein alignments organised as structural superfamilies , 2004, BMC Bioinformatics.

[4]  M. Gromiha,et al.  Clusters in α/β barrel proteins: Implications for protein structure, function, and folding: A graph theoretical approach , 2001, Proteins.

[5]  P. Kraulis A program to produce both detailed and schematic plots of protein structures , 1991 .

[6]  G. Petsko,et al.  The evolution of alpha/beta barrel enzymes. , 1990, Trends in biochemical sciences.

[7]  K. Nishikawa,et al.  Radial locations of amino acid residues in a globular protein: correlation with the sequence. , 1986, Journal of biochemistry.

[8]  Ponnuthurai N. Suganthan,et al.  SMotif: a server for structural motifs in proteins , 2007, Bioinform..

[9]  Ramanathan Sowdhamini,et al.  SSToSS - Sequence-Structural Templates of Single-Member Superfamilies , 2006, Silico Biol..

[10]  John P. Overington,et al.  HOMSTRAD: A database of protein structure alignments for homologous families , 1998, Protein science : a publication of the Protein Society.

[11]  A G Murzin,et al.  SCOP: a structural classification of proteins database for the investigation of sequences and structures. , 1995, Journal of molecular biology.

[12]  Gregory A. Petsko,et al.  The evolution of a/ barrel enzymes , 1990 .

[13]  R A Sayle,et al.  RASMOL: biomolecular graphics for all. , 1995, Trends in biochemical sciences.

[14]  Saikat Chakrabarti,et al.  Regions of minimal structural variation among members of protein domain superfamilies: application to remote homology detection and modelling using distant relationships , 2004, FEBS letters.

[15]  Saikat Chakrabarti,et al.  SMoS: a database of structural motifs of protein superfamilies. , 2003, Protein engineering.

[16]  Ramanathan Sowdhamini,et al.  SCANMOT: searching for similar sequences using a simultaneous scan of multiple sequence motifs , 2005, Nucleic Acids Res..

[17]  Ramanathan Sowdhamini,et al.  Improvement of alignment accuracy utilizing sequentially conserved motifs , 2004, BMC Bioinformatics.