1j1l

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Revision as of 15:30, 12 November 2007

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spinqualitylabelsall models 1j1l, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of human Pirin: a Bcl-3 and Nuclear factor I interacting protein and a cupin superfamily member

Overview

Pirin is a newly identified nuclear protein that interacts with the, oncoprotein B-cell lymphoma 3-encoded (Bcl-3) and nuclear factor I (NFI)., The crystal structure of human Pirin at 2.1-A resolution shows it to be a, member of the functionally diverse cupin superfamily. The structure, comprises two beta-barrel domains, with an Fe(II) cofactor bound within, the cavity of the N-terminal domain. These findings suggest an enzymatic, role for Pirin, most likely in biological redox reactions involving, oxygen, and provide compelling evidence that Pirin requires the, participation of the metal ion for its interaction with Bcl-3 to, co-regulate the NF-kappaB transcription pathway and the interaction with, NFI in DNA replication. Substitution of iron by heavy metals thus provides, a novel pathway for these metals to directly influence gene transcription., The structure suggests an interesting new role of iron in biology and that, Pirin may be involved in novel mechanisms of gene regulation.

About this Structure

1J1L is a Single protein structure of sequence from Homo sapiens with FE2 as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of human pirin: an iron-binding nuclear protein and transcription cofactor., Pang H, Bartlam M, Zeng Q, Miyatake H, Hisano T, Miki K, Wong LL, Gao GF, Rao Z, J Biol Chem. 2004 Jan 9;279(2):1491-8. Epub 2003 Oct 22. PMID:14573596

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