PDBsum entry: 3dju

Transcription

PDB-id: 3dju

Main view

Contents

Description

Header details

Header records

References

PROCHECK

Protein chain

121 a.a. *

Waters ×49

* Residue conservation analysis

Tools

Clefts Calculation

Right view	Bottom view

PDB id:

3dju

Name:

Transcription

Title:

Crystal structure of human btg2

Structure:

Protein btg2. Chain: b. Fragment: unp residues 7-128. Synonym: ngf-inducible anti-proliferative protein pc3. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: btg2, b-cell translocation gene 2. Expressed in: escherichia coli. Expression_system_taxid: 562.

UniProt:

P78543 (BTG2_HUMAN)

Seq:

158 a.a.

Struc:

121 a.a.

Key:

PfamA domain

Secondary structure

Resolution:

2.26Å

R-factor:

0.198

R-free:

0.263

Authors:

X.Yang,M.Morita,H.Wang,T.Suzuki,M.Bartlam,T.Yamamoto

Key ref:

X.Yang et al. (2008). Crystal structures of human BTG2 and mouse TIS21 involved in suppression of CAF1 deadenylase activity.. Nucleic Acids Res, 36, 6872-6881. [PubMed id: 18974182] [DOI: 10.1093/nar/gkn825]

Date:

24-Jun-08

Release date:

11-Nov-08

Related entries:

3djn

Quick_links

Procheck

Clefts

Surface

Key reference

DOI no: 10.1093/nar/gkn825

Nucleic Acids Res 36:6872-6881 (2008)

PubMed id: 18974182

Crystal structures of human BTG2 and mouse TIS21 involved in suppression of CAF1 deadenylase activity.

X.Yang, M.Morita, H.Wang, T.Suzuki, W.Yang, Y.Luo, C.Zhao, Y.Yu, M.Bartlam, T.Yamamoto, Z.Rao.

ABSTRACT

BTG2 is the prototypical member of the TOB family and is known to be involved in cell growth, differentiation and DNA repair. As a transcriptional co-regulator, BTG2 interacts with CCR4-associated factor 1 (CAF1) and POP2 (CALIF), which are key components of the general CCR4/NOT multi-subunit transcription complex, and which are reported to play distinct roles as nucleases involved in mRNA deadenylation. Here we report the crystal structures of human BTG2 and mouse TIS21 to 2.3 A and 2.2 A resolution, respectively. The structures reveal the putative CAF1 binding site. CAF1 deadenylase assays were performed with wild-type BTG2 and mutants that disrupt the interaction with CAF1. The results reveal the suppressive role of BTG2 in the regulation of CAF1 deadenylase activity. Our study provides insights into the formation of the BTG2-CAF1 complex and the potential role of BTG2 in the regulation of CAF1.