Representing and recognizing protein active sites sequence motif (1D motif) and structural motif (3D motif) is an important topic for predicting and designing protein function. Prevalent methods for extracting and sea...Representing and recognizing protein active sites sequence motif (1D motif) and structural motif (3D motif) is an important topic for predicting and designing protein function. Prevalent methods for extracting and searching 3D motif always consider residue as the minimal unit, which have limited sensitivity. Here we present a new spatial representation of protein active sites, called 'functional-group 3D motif', based on the fact that the functional groups inside a residue contribute mostly to its function. Relevant algorithm and computer program are developed, which could be widely used in the function prediction and the study of structural-function relationship of proteins. As a test, we defined a functional-group 3D motif of the catalytic triad and oxyanion hole with the structure of porcine trypsin (PDB code: 1mct) as the template. With our motif-searching program, we successfully found similar sub-structures in trypsins, subtilisins and α/β hydrolases, which show distinct folds but share展开更多
The function of a protein molecule is greatly influenced by its three-dimensional （3D） structure and therefore structure prediction will help identify its biological function. We have updated Sequence, Motif and Str...The function of a protein molecule is greatly influenced by its three-dimensional （3D） structure and therefore structure prediction will help identify its biological function. We have updated Sequence, Motif and Structure （SMS）, the database of structurally rigid peptide fragments, by combining amino acid sequences and the corre- sponding 3D atomic coordinates of non-redundant （25%） and redundant （90%） protein chains available in the Protein Data Bank （PDB）. SMS 2.0 provides information pertaining to the peptide fragments of length 5-14 resi- dues. The entire dataset is divided into three categories, namely, same sequence motifs having similar, intermedi- ate or dissimilar 3D structures. Further, options are provided to facilitate structural superposition using the pro- gram structural alignment of multiple proteins （STAMP） and the popular JAVA plug-in （Jmol） is deployed for visualization. In addition, functionalities are provided to search for the occurrences of the sequence motifs in other structural and sequence databases like PDB, Genome Database （GDB）, Protein Information Resource （PIR） and Swiss-Prot. The updated database along with the search engine is available over the World Wide Web through the following URL http：//cluster.physics.iisc.ernet.in/sms/.展开更多
文摘Representing and recognizing protein active sites sequence motif (1D motif) and structural motif (3D motif) is an important topic for predicting and designing protein function. Prevalent methods for extracting and searching 3D motif always consider residue as the minimal unit, which have limited sensitivity. Here we present a new spatial representation of protein active sites, called 'functional-group 3D motif', based on the fact that the functional groups inside a residue contribute mostly to its function. Relevant algorithm and computer program are developed, which could be widely used in the function prediction and the study of structural-function relationship of proteins. As a test, we defined a functional-group 3D motif of the catalytic triad and oxyanion hole with the structure of porcine trypsin (PDB code: 1mct) as the template. With our motif-searching program, we successfully found similar sub-structures in trypsins, subtilisins and α/β hydrolases, which show distinct folds but share
基金supported by a research grant from the Department of Information Technology (DIT) awarded to KS
文摘The function of a protein molecule is greatly influenced by its three-dimensional （3D） structure and therefore structure prediction will help identify its biological function. We have updated Sequence, Motif and Structure （SMS）, the database of structurally rigid peptide fragments, by combining amino acid sequences and the corre- sponding 3D atomic coordinates of non-redundant （25%） and redundant （90%） protein chains available in the Protein Data Bank （PDB）. SMS 2.0 provides information pertaining to the peptide fragments of length 5-14 resi- dues. The entire dataset is divided into three categories, namely, same sequence motifs having similar, intermedi- ate or dissimilar 3D structures. Further, options are provided to facilitate structural superposition using the pro- gram structural alignment of multiple proteins （STAMP） and the popular JAVA plug-in （Jmol） is deployed for visualization. In addition, functionalities are provided to search for the occurrences of the sequence motifs in other structural and sequence databases like PDB, Genome Database （GDB）, Protein Information Resource （PIR） and Swiss-Prot. The updated database along with the search engine is available over the World Wide Web through the following URL http：//cluster.physics.iisc.ernet.in/sms/.
