Crystallization and preliminary crystallographic studies of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain
Authors: Razeto, Adelia; Pfitzner, Edith; Becker, Stefan
Source: Acta Crystallographica Section D, Volume 60, Number 3, March 2004 , pp. 550-552(3)
Publisher: Blackwell Publishing
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Abstract:
Signal transducer and activator of transcription 6 (STAT6) regulates transcriptional activation in response to interleukin-4 (IL-4) by direct interaction with coactivators. Among them, NCoA-1, a member of the p160/steroid receptor coactivator (SRC) family, has been found to bind to STAT6 with the region B of its putative Per-Arnt-Sim (PAS) domain. STAT6 interacts specifically with NCoA-1 via an LXXLL motif in its transactivation domain. Crystals of the NCoA-1(257-385) domain in complex with the STAT6(794-814) LXXLL motif were obtained in two hexagonal space groups. The crystals in space group P61, with unit-cell parameters a = 61.7, b = 61.7, c = 146.5 Å, α = β = 90, γ = 120°, diffract to 2.8 Å at a home source. Crystals belonging to space group P62, with unit-cell parameters a = 62.0, b = 62.0, c = 73.6 Å, α = β = 90, γ = 120°, diffract to 1.8 Å at a synchrotron source.Keywords: STAT6; Per-Arnt-Sim domain; NCoA-1; SRC family
Document Type: Research article
DOI: 10.1107/S0907444903029378
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