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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Oct 1;66(Pt 10):1218-25. doi: 10.1107/S1744309109050416. Epub 2010 Mar 5.

Structures of the first representatives of Pfam family PF06938 (DUF1285) reveal a new fold with repeated structural motifs and possible involvement in signal transduction.

Author information

1
Stanford Synchrotron Radiation ightsource, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.

Abstract

The crystal structures of SPO0140 and Sbal_2486 were determined using the semiautomated high-throughput pipeline of the Joint Center for Structural Genomics (JCSG) as part of the NIGMS Protein Structure Initiative (PSI). The structures revealed a conserved core with domain duplication and a superficial similarity of the C-terminal domain to pleckstrin homology-like folds. The conservation of the domain interface indicates a potential binding site that is likely to involve a nucleotide-based ligand, with genome-context and gene-fusion analyses additionally supporting a role for this family in signal transduction, possibly during oxidative stress.

PMID:
20944214
PMCID:
PMC2954208
DOI:
10.1107/S1744309109050416
[Indexed for MEDLINE]
Free PMC Article

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