Published in
Oxford University Press, Nucleic Acids Research, Web Server(32), p. W356-W359, 2004
DOI: 10.1093/nar/gkh394
Links
- ORCID
- Oxford University Press
- [www.ncbi.nlm.nih.gov] | PDF
- [scholarbank.nus.edu.sg]
- [europepmc.org] | PDF
- [www.researchgate.net] | PDF
- [www.ncbi.nlm.nih.gov] | PDF
- [www.ncbi.nlm.nih.gov] | PDF
- [citeseerx.ist.psu.edu] | PDF
- [nar.oxfordjournals.org] | PDF
Tools
SDPMOD: an automated comparative modeling server for small disulfide-bonded proteins
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Abstract
Small disulfide-bonded proteins (SDPs) are rich sources for therapeutic drugs. Designing drugs from these proteins requires three-dimensional structural information, which is only available for a subset of these proteins. SDPMOD addresses this deficit in structural information by providing a freely available automated comparative modeling service to the research community. For expert users, SDPMOD offers a manual mode that permits the selection of a desired template as well as a semi-automated mode that allows users to select the template from a suggested list. Besides the selection of templates, expert users can edit the target–template alignment, thus allowing further customization of the modeling process. Furthermore, the web service provides model stereochemical quality evaluation using PROCHECK. SDPMOD is freely accessible to academic users via the web interface at http://proline.bic.nus.edu.sg/sdpmod.