PDBsum entry 3cwg

Transcription

PDB id: 3cwg

Contents

Protein chains

501 a.a. *

* Residue conservation analysis

PDB id:

3cwg

Name:

Transcription

Title:

Unphosphorylated mouse stat3 core fragment

Structure:

Signal transducer and activator of transcription 3. Chain: a, b. Fragment: stat3 core fragment, unp residues (127-688). Synonym: acute-phase response factor. Engineered: yes

Source:

Mus musculus. Mouse. Gene: stat3, aprf. Expressed in: escherichia coli.

Resolution:

3.05Å R-factor: 0.250 R-free: 0.269

Authors:

Z.Ren,X.Mao,C.Mertens,R.Krishnaraj,J.Qin,P.K.Mandal,M.J.Romanowshi, J.S.Mcmurray

Key ref:

Z.Ren et al. (2008). Crystal structure of unphosphorylated STAT3 core fragment. Biochem Biophys Res Commun, 374, 1-5. PubMed id: 18433722

Date:

21-Apr-08 Release date: 01-Jul-08

Protein chains

P42227  (STAT3_MOUSE) -  Signal transducer and activator of transcription 3 from Mus musculus

Seq: 770 a.a.

Struc: 501 a.a.

Biochem Biophys Res Commun 374:1-5 (2008)

PubMed id: 18433722

Crystal structure of unphosphorylated STAT3 core fragment.

Z.Ren, X.Mao, C.Mertens, R.Krishnaraj, J.Qin, P.K.Mandal, M.J.Romanowski, J.S.McMurray, X.Chen.

ABSTRACT

Signal transducers and activators of transcription (STATs) are latent cytoplasmic transcriptional factors that play an important role in cytokine and growth factor signaling. Here we report a 3.05 A-resolution crystal structure of an unphosphorylated STAT3 core fragment. The overall monomeric structure is very similar to that of the phosphorylated STAT3 core fragment. However, the dimer interface observed in the unphosphorylated STAT1 core fragment structure is absent in the STAT3 structure. Solution studies further demonstrate that the core fragment of STAT3 is primarily monomeric. Mutations corresponding to those in STAT1, which lead to disruption of the core fragment interface and prolonged tyrosine phosphorylation, show little or no effect on the tyrosine phosphorylation kinetics of STAT3. These results highlight the structural and biochemical differences between STAT3 and STAT1, and suggest different regulation mechanisms of these two proteins.