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Bioinformatics. 2016 Jun 1;32(11):1709-15. doi: 10.1093/bioinformatics/btw032. Epub 2016 Jan 30.

Library of binding protein scaffolds (LibBP): a computational platform for selection of binding protein scaffolds.

Author information

1
Department of Bio and Brain Engineering, KAIST, Daejeon 305-338, South Korea.

Abstract

MOTIVATION:

Developments in biotechnology have enabled the in vitro evolution of binding proteins. The emerging limitations of antibodies in binding protein engineering have led to suggestions for other proteins as alternative binding protein scaffolds. Most of these proteins were selected based on human intuition rather than systematic analysis of the available data. To improve this strategy, we developed a computational framework for finding desirable binding protein scaffolds by utilizing protein structure and sequence information.

RESULTS:

For each protein, its structure and the sequences of evolutionarily-related proteins were analyzed, and spatially contiguous regions composed of highly variable residues were identified. A large number of proteins have these regions, but leucine rich repeats (LRRs), histidine kinase domains and immunoglobulin domains are predominant among them. The candidates suggested as new binding protein scaffolds include histidine kinase, LRR, titin and pentapeptide repeat protein.

AVAILABILITY AND IMPLEMENTATION:

The database and web-service are accessible via http://bcbl.kaist.ac.kr/LibBP CONTACT: kds@kaist.ac.krSupplementary data: Supplementary data are available at Bioinformatics online.

PMID:
26826717
DOI:
10.1093/bioinformatics/btw032
[Indexed for MEDLINE]

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