Related ArticlesNMR structure of the first PHD finger of autoimmune regulator protein (AIRE1). Insights into autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy (APECED) disease.
J Biol Chem. 2005 Mar 25;280(12):11505-12
Authors: Bottomley MJ, Stier G, Pennacchini D, Legube G, Simon B, Akhtar A, Sattler M, Musco G
Mutations in the autoimmune regulator protein AIRE1 cause a monogenic autosomal recessively inherited disease: autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy (APECED). AIRE1 is a multidomain protein that harbors two plant homeodomain (PHD)-type zinc fingers. The first PHD finger of AIRE1 is a mutational hot spot, to which several pathological point mutations have been mapped. Using heteronuclear NMR spectroscopy, we determined the solution structure of the first PHD finger of AIRE1 (AIRE1-PHD1), and characterized the peptide backbone mobility of the domain. We performed a conformational analysis of pathological AIRE1-PHD1 mutants that allowed us to rationalize the structural impact of APECED-causing mutations and to identify an interaction site with putative protein ligands of the AIRE1-PHD1 domain. The structure unequivocally exhibits the canonical PHD finger fold, with a highly conserved tryptophan buried inside the structure. The PHD finger is stabilized by two zinc ions coordinated in an interleaved (cross-brace) scheme. This zinc coordination resembles RING finger domains, which can function as E3 ligases in the ubiquitination pathway. Based on this fold similarity, it has been suggested that PHD fingers might also function as E3 ligases, although this hypothesis is controversial. At variance to a previous report, we could not find any evidence that AIRE1-PHD1 has an intrinsic E3 ubiquitin ligase activity, nor detect any direct interaction between AIRE1-PHD1 and its putative cognate E2. Consistently, we show that the AIRE1-PHD1 structure is clearly distinct from the RING finger fold. Our results point to a function of the AIRE1-PHD1 domain in protein-protein interactions, which is impaired in some APECED mutations.
[NMR paper] NMR and molecular dynamics studies of an autoimmune myelin basic protein peptide and
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Eur J Biochem. 2004 Aug;271(16):3399-413
Authors: Tzakos AG, Fuchs P, van Nuland NA, Troganis A, Tselios T, Deraos S, Matsoukas J, Gerothanassis IP, Bonvin AM
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Authors: Stote RH, Kellenberger E, Muller H, Bombarda E, Roques BP, Kieffer B, Mély Y
The nucleocapsid protein (NCp7) of human...
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Chembiochem. 2003 Mar 3;4(2-3):171-80
Authors: Isernia C, Bucci E, Leone M, Zaccaro L, Di Lello P, Digilio G, Esposito S, Saviano M, Di Blasio B, Pedone C, Pedone PV, Fattorusso R
Zinc finger domains of the classical type represent the most abundant DNA binding domains in eukaryotic transcription factors. Plant proteins...
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J Biol Chem. 2003 Apr 25;278(17):15341-8
Authors: Katoh S, Hong C, Tsunoda Y, Murata K, Takai R, Minami E, Yamazaki T, Katoh E
EL5, a RING-H2 finger protein, is rapidly induced by...
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J Mol Biol. 2001 Nov 16;314(1):129-38
Authors: Shekhtman A, Ghose R, Wang D, Cole PA, Cowburn D
Csk (C-terminal Src kinase), a protein tyrosine kinase, consisting of the Src homology 2 and 3 (SH2 and SH3) domains and a catalytic domain,...
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Biochemistry. 2001 Aug 14;40(32):9596-604
Authors: Schüler W, Kloiber K, Matt T, Bister K, Konrat R
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Biochemistry. 1999 Oct 5;38(40):12984-94
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NMR assignments for the Sinorhizobium meliloti response regulator Sma0114.
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Biomol NMR Assign. 2010 Oct 10;
Authors: Sheftic SR, Garcia PP, Robinson VL, Gage DJ, Alexandrescu AT
Response regulators are terminal ends of bacterial two-component systems that undergo extensive structural reorganization in response to phosphoryl transfer from their cognate histidine kinases. The response regulator encoded by the gene sma0114 of Sinorhizobium meliloti is a part of...
NMR structure of the first PHD finger of autoimmune regulator protein (AIRE1). Insigh
Linear Mode
