PDBsum entry 1jjs

Transcription

PDB id: 1jjs

Contents

Protein chain

42 a.a.

PDB id:

1jjs

Name:

Transcription

Title:

Nmr structure of ibid, a domain of cbp/p300

Structure:

Creb-binding protein. Chain: a. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Gene: cbp. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

12 models

Authors:

C.H.Lin,B.J.Hare,G.Wagner,S.C.Harrison,T.Maniatis,E.Fraenkel

Key ref:

C.H.Lin et al. (2001). A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies. Mol Cell, 8, 581-590. PubMed id: 11583620 DOI: 10.1016/S1097-2765(01)00333-1

Date:

09-Jul-01 Release date: 03-Oct-01

Protein chain

P45481  (CBP_MOUSE) -  Histone lysine acetyltransferase CREBBP from Mus musculus

Seq: 2441 a.a.

Struc: 42 a.a.

Enzyme reactions

• Enzyme class 1: E.C.2.3.1.- - ?????
• Enzyme class 2: E.C.2.3.1.48 - histone acetyltransferase.
• Reaction: L-lysyl-[protein] + acetyl-CoA = N₆-acetyl-L-lysyl-[protein] + CoA + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1016/S1097-2765(01)00333-1

Mol Cell 8:581-590 (2001)

PubMed id: 11583620

A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies.

C.H.Lin, B.J.Hare, G.Wagner, S.C.Harrison, T.Maniatis, E.Fraenkel.

ABSTRACT

The transcriptional coactivators CBP and p300 are critical regulators of metazoan gene expression. They associate with many different DNA-bound transcription factors through small, conserved domains. We have identified a compactly folded 46 residue domain in CBP and p300, the IRF-3 binding domain (IBiD), and we have determined its structure by NMR. It has a helical framework containing an apparently flexible polyglutamine loop that participates in ligand binding. Spectroscopic data indicate that induced folding accompanies association of IBiD with its partners, which exhibit no evident sequence similarities. We demonstrate the significance both in vitro and in vivo of interactions between IBiD and a number of diverse partners. Thus, IBiD is an important contributor to signal integration by CBP and p300.

Selected figure(s)

Figure 5.
Figure 5. IRF-3, KSHV IRF-1, TIF-2, and E1A Compete for Binding to IBiD(A) CAT reporter activity measured in extracts of cells transfected with the indicated plasmids (E1A 12S WT or H3N: 1 μg; IRF-3 E5: 0.5 μg and 1 μg; KSHV IRF-1: 0.5 μg and 1 μg) or infected with Sendai virus.(B) In vitro pull-down analysis using immobilized IBiD showing the competition for binding to IBiD between TIF-2 (cold) and either IRF-3 E5 or KSHV IRF-1 (^35S-labeled). The percentages of IRF-3 E5 and KSHV IRF-1 that remained bound are shown.(C) CAT assays showing the inhibitory effect of either WT or H3N E1A 12S on virus induction of (PRDIII-I)[3]. Amounts of effector constructs transfected: 0.5 and 1 μg. Immunoblot analysis (inset) using an α-E1A antibody (Santa Cruz) indicates the expression levels of these E1A constructs.(D) CAT assays showing the inhibitory effect of either WT or H3N E1A 12S, and KSHV IRF-1 on the transcription driven by Gal4-IRF-3 E5. Amounts of effector constructs transfected: Gal4-IRF-3 E5, 50 ng; viral gene constructs, 0.25, 0.5, and 1 μg

Figure 6.
Figure 6. Flexible Domain Organization of CBP/p300Schematic diagram illustrating how flexible tethers may permit CBP/p300 molecules to adapt to different enhancers. Binding of ligands can indirectly modify acetyltransferase activity by causing domain rearrangements. Two mechanisms by which phosphorylation of a ligand regulates its binding to CBP/p300 are also shown

The above figures are reprinted by permission from Cell Press: Mol Cell (2001, 8, 581-590) copyright 2001.

Figures were selected by an automated process.