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Crystal structure of human Pirin: a Bcl-3 and Nuclear factor I interacting protein and a cupin superfamily memberCrystal structure of human Pirin: a Bcl-3 and Nuclear factor I interacting protein and a cupin superfamily member
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPirin 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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