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1OJ5

Crystal structure of the Nco-A1 PAS-B domain bound to the STAT6 transactivation domain LXXLL motif

Summary for 1OJ5
Entry DOI10.2210/pdb1oj5/pdb
Related1K74 1K7L 2PRG
DescriptorSTEROID RECEPTOR COACTIVATOR 1A, SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION 6, IODIDE ION, ... (4 entities in total)
Functional Keywordstranscriptional coactivator, complex, lxxll motif, transcriptional regulation, stat6, pas domain, il-4 stat
Biological sourceMUS MUSCULUS (MOUSE)
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Cellular locationCytoplasm: P42226
Total number of polymer chains2
Total formula weight17057.16
Authors
Razeto, A.,Ramakrishnan, V.,Giller, K.,Lakomek, N.,Carlomagno, T.,Griesinger, C.,Lodrini, M.,Litterst, C.M.,Pftizner, E.,Becker, S. (deposition date: 2003-07-02, release date: 2004-02-12, Last modification date: 2024-05-08)
Primary citationRazeto, A.,Ramakrishnan, V.,Litterst, C.M.,Giller, K.,Griesinger, C.,Carlomagno, T.,Lakomek, N.,Heimburg, T.,Lodrini, M.,Pfitzner, E.,Becker, S.
Structure of the Ncoa-1/Src-1 Pas-B Domain Bound to the Lxxll Motif of the Stat6 Transactivation Domain
J.Mol.Biol., 336:319-, 2004
Cited by
PubMed Abstract: Signal transducer and activator of transcription 6 (STAT6) regulates transcriptional activation in response to interleukin-4 (IL-4) by direct interaction with coactivators. The CREB-binding protein (p300/CBP) and the nuclear coactivator 1 (NCoA-1), a member of the p160/steroid receptor coactivator family, bind independently to specific regions of the STAT6 transactivation domain and act as coactivators. The interaction between STAT6 and NCoA-1 is mediated by an LXXLL motif in the transactivation domain of STAT6. To define the mechanism of coactivator recognition, we determined the crystal structure of the NCoA-1 PAS-B domain in complex with the STAT6 LXXLL motif. The amphipathic, alpha-helical STAT6 LXXLL motif binds mostly through specific hydrophobic interactions to NCoA-1. A single amino acid of the NCoA-1 PAS-B domain establishes hydrophilic interactions with the STAT6 peptide. STAT6 interacts only with the PAS-B domain of NCoA-1 but not with the homologous regions of NCoA-2 and NCoA-3. The residues involved in binding the STAT6 peptide are strongly conserved between the different NCoA family members. Therefore surface complementarity between the hydrophobic faces of the STAT6 fragment and of the NCoA-1 PAS-B domain almost exclusively defines the binding specificity between the two proteins.
PubMed: 14757047
DOI: 10.1016/J.JMB.2003.12.057
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.21 Å)
Structure validation

237735

数据于2025-06-18公开中

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