PDBsum entry: 1pzu

Transcription/DNA

PDB id: 1pzu

Contents

Protein chains

(+ 0 more) 276 a.a. *

DNA/RNA

* Residue conservation analysis

PDB id:

1pzu

Name:

Transcription/DNA

Title:

An asymmetric nfat1-rhr homodimer on a pseudo-palindromic, kappa-b site

Structure:

5'-d( Tp Tp Gp Ap Gp Gp Ap Ap Tp Tp Tp Cp Cp A)- 3'. Chain: x, v, t. Engineered: yes. 5'-d( Ap Ap Tp Gp Gp Ap Ap Ap Tp Tp Cp Cp Tp C)- 3'. Chain: y, z, w. Engineered: yes. Nuclear factor of activated t-cells, cytoplasmic

Source:

Synthetic: yes. Homo sapiens. Human. Organism_taxid: 9606. Gene: nfat1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Tetramer (from PQS)

Resolution:

3.10Å R-factor: 0.296 R-free: 0.319

Authors:

L.Jin,P.Sliz,L.Chen,F.Macian,A.Rao,P.G.Hogan,S.C.Harrison

Key ref:

L.Jin et al. (2003). An asymmetric NFAT1 dimer on a pseudo-palindromic kappa B-like DNA site. Nat Struct Biol, 10, 807-811. PubMed id: 12949491 DOI: 10.1038/nsb975

Date:

14-Jul-03 Release date: 09-Sep-03

Protein chains

Q13469  (NFAC2_HUMAN) -  Nuclear factor of activated T-cells, cytoplasmic 2

Seq: 925 a.a.

Struc: 276 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: nucleus (1 term)
• Biological process: regulation of transcription (2 terms)
• Biochemical function: transcription factor activity (1 term)

DOI no: 10.1038/nsb975

Nat Struct Biol 10:807-811 (2003)

PubMed id: 12949491

An asymmetric NFAT1 dimer on a pseudo-palindromic kappa B-like DNA site.

L.Jin, P.Sliz, L.Chen, F.Macián, A.Rao, P.G.Hogan, S.C.Harrison.

ABSTRACT

The crystal structure of the NFAT1 Rel homology region (RHR) bound to a pseudo-palindromic DNA site reveals an asymmetric dimer interaction between the RHR-C domains, unrelated to the contact seen in Rel dimers such as NF kappa B. Binding studies with a form of the NFAT1 RHR defective in the dimer contact show loss of cooperativity and demonstrate that the same interaction is present in solution. The structure we have determined may correspond to a functional NFAT binding mode at palindromic sites of genes induced during the anergic response to weak TCR signaling.

Selected figure(s)

Figure 1.
Figure 1. Structures of members of the RHR family of transcription factors bound to DNA. (a -c) Views along the DNA axis of (a) the p50 homodimer of NF B on a B site (b) the NFAT1 -RHR -Fos-Jun ternary complex on the ARRE2 site and (c) one of the NFAT1 dimers from the present crystal structure. The RHR-N domain is yellow and its symmetry mate light yellow; the RHR-C domain is green and its partner light green; Fos, red; Jun, blue. Colors here are used throughout the rest of the figures.

Figure 2.
Figure 2. View of the three crystallographically nonequivalent dimers in the orthorhombic crystal form of the NFAT1 dimer -DNA complex. (a) One asymmetric unit of the P2[1]2[1]2[1] crystal, with the non-crystallographic three-fold screw axis shown. The view is normal to the DNA axis. (b -d) Each of the three crystallographically distinct dimers, viewed along the DNA axis, with the RHR-N domains in corresponding orientations. The inset diagrams show the asymmetry of the RHR-C interactions. The orientation of the asymmetric RHR-C pair in b is opposite from those in c and d. The tilt of the RHR-C dimer axis varies among the dimers by up to 10°.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2003, 10, 807-811) copyright 2003.

Figures were selected by the author.