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1SB0

Solution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb

1SB0 の概要
エントリーDOI10.2210/pdb1sb0/pdb
NMR情報BMRB: 6095
分子名称protein CBP, protein c-Myb (2 entities in total)
機能のキーワードcreb-binding protein; transcriptional activation; constitutive activation; lxxll motif; myb; kix, transcription
由来する生物種Mus musculus (house mouse)
詳細
細胞内の位置Cytoplasm (By similarity): P45481
Nucleus: P06876
タンパク質・核酸の鎖数2
化学式量合計13301.33
構造登録者
Zor, T.,De Guzman, R.N.,Dyson, H.J.,Wright, P.E. (登録日: 2004-02-09, 公開日: 2004-04-13, 最終更新日: 2024-05-22)
主引用文献Zor, T.,De Guzman, R.N.,Dyson, H.J.,Wright, P.E.
Solution Structure of the KIX Domain of CBP Bound to the Transactivation Domain of c-Myb
J.Mol.Biol., 337:521-534, 2004
Cited by
PubMed Abstract: The hematopoietic transcription factor c-Myb activates transcription of target genes through direct interactions with the KIX domain of the co-activator CBP. The solution structure of the KIX domain in complex with the activation domain of c-Myb reveals a helical structure very similar to that adopted by KIX in complex with the phosphorylated kinase inducible domain (pKID) of CREB. While pKID contains two helices, alphaA and alphaB, which interact with KIX, the structure of bound c-Myb reveals a single bent amphipathic helix that binds in the same hydrophobic groove as the alphaB helix of pKID. The affinity of c-Myb for KIX is lower than that of pKID, and relies more heavily on optimal interactions of the single helix of c-Myb with residues in the hydrophobic groove. In particular, a deep hydrophobic pocket in KIX accounts for more than half the interactions with c-Myb observed by NMR. A bend in the alpha-helix of c-Myb enables a critical leucine side-chain to penetrate into this pocket more deeply than the equivalent leucine residue of pKID. The components that mediate the higher affinity of pKID for KIX, i.e. the phosphate group and the alphaA helix, are absent from c-Myb. Results from isothermal titration calorimetry, together with the structural data, point to a key difference between the two complexes in optimal pH for binding, as a result of differential pH-dependent interactions with histidine residues of KIX. These results explain the structural and thermodynamic basis for the observed constitutive versus inducible activation properties of c-Myb and CREB.
PubMed: 15019774
DOI: 10.1016/j.jmb.2004.01.038
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 1sb0
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-06に公開中

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