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A biophysical characterization of the folded domains of KCTD12: insights into interaction with the GABA(B2) receptor (109 visite)

Correale S, Esposito C, Pirone L, Vitagliano L, Di Gaetano S, Pedone E

Journal Of Molecular Recognition (ISSN: 0952-3499, 0952-2349), 2013 Oct; 26(10): 488-495.

Tipo di articolo: Journal Article,

Impact factor: 2.337

Impact factor a 5 anni: 2.483

Parole chiave: Cd Spectroscopy, Gabab2 Receptor, Interaction Studies, Kctd12, Oligomerization State, Peptide Design, 4 Aminobutyric Acid A Receptor, Gabrr2 Protein, Human, Kctd12 Protein, Recombinant Protein, Amino Acid Sequence, Article, Binding Site, Chemistry, Escherichia Coli, Genetics, Molecular Cloning, Molecular Genetics, Protein Binding, Protein Domain, Protein Folding, Protein Multimerization, Protein Secondary Structure, Molecular Sequence Data, Protein Interaction Domains And Motifs, Protein Structure,

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84883301541&partnerID=40&md5=f159f67fb1883c95f33be9ace58b0e75

Recent investigations have shown that members of the KCTD family play important roles in fundamental biological processes. Despite their roles, very limited information is available on their structures and molecular organization. By combining different experimental and theoretical techniques, we have here characterized the two folded domains of KCTD12, an integral component and modulator of the GABA (B2) receptor. Secondary prediction methods and CD spectroscopy have shown that the N-terminal domain KCTD12 (BTB) assumes an / structure, whereas the C-terminal domain KCTD12 (H1) is predominantly characterized by a -structure. Binding assays indicate that the two domains independently expressed show a good affinity for each other. This suggests that the overall protein is likely endowed with a rather compact structure with two interacting structured domains joint by a long disordered region. Notably, both KCTD12 (BTB) and KCTD12 (H1) are tetrameric when individually expressed. This finding could modify the traditional view that ascribes only to POZ/BTB domain a specific oligomerization role. The first quantification of the affinity of KCTD12 (POZ/BTB) for the C-terminal region of GABA (B2) shows that it falls in the low micromolar range. Interestingly, we also demonstrate that a GABA (B2) -related peptide is able to bind KCTD12 (BTB) with a very high affinity. This peptide may represent a useful tool for modulating KCTD12/GABA (B2) interaction in vitro and may also constitute the starting point for the development of peptidomimetic compounds with a potential for therapeutic applications. Copyright (c) 2013 John Wiley & Sons, Ltd
*** IBB - CNR ***

Istituto di Biostrutture e Bioimmagini, CNR, via Mezzocannone 16, 80134 Napoli, Italy

Kedrion S. p. A, 80029 S. Antimo, Napoli, Italy

DFM Scarl, via Mezzocannone 16, 80134 Napoli, Italy

Institute of Crystallography, CNR, 70126 Bari, Italy

Kedrion S.p.A, 80029 S. Antimo, Napoli, Italy
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3 Records (2 escludendo Abstract e Conferenze).
Impact factor totale: 11.144 (6.956 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 13.604 (6.441 escludendo Abstract e Conferenze).

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