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STRALCP--structure alignment-based clustering of proteins.


ABSTRACT: Protein structural annotation and classification is an important and challenging problem in bioinformatics. Research towards analysis of sequence-structure correspondences is critical for better understanding of a protein's structure, function, and its interaction with other molecules. Clustering of protein domains based on their structural similarities provides valuable information for protein classification schemes. In this article, we attempt to determine whether structure information alone is sufficient to adequately classify protein structures. We present an algorithm that identifies regions of structural similarity within a given set of protein structures, and uses those regions for clustering. In our approach, called STRALCP (STRucture ALignment-based Clustering of Proteins), we generate detailed information about global and local similarities between pairs of protein structures, identify fragments (spans) that are structurally conserved among proteins, and use these spans to group the structures accordingly. We also provide a web server at http://as2ts.llnl.gov/AS2TS/STRALCP/ for selecting protein structures, calculating structurally conserved regions and performing automated clustering.

SUBMITTER: Zemla A 

PROVIDER: S-EPMC2190701 | biostudies-literature | 2007

REPOSITORIES: biostudies-literature

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STRALCP--structure alignment-based clustering of proteins.

Zemla Adam A   Geisbrecht Brian B   Smith Jason J   Lam Marisa M   Kirkpatrick Bonnie B   Wagner Mark M   Slezak Tom T   Zhou Carol Ecale CE  

Nucleic acids research 20071126 22


Protein structural annotation and classification is an important and challenging problem in bioinformatics. Research towards analysis of sequence-structure correspondences is critical for better understanding of a protein's structure, function, and its interaction with other molecules. Clustering of protein domains based on their structural similarities provides valuable information for protein classification schemes. In this article, we attempt to determine whether structure information alone i  ...[more]

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