Design, synthesis and characterization of a peptide able to bind proteins of the KCTD family: implications for KCTD - cullin 3 recognition(524 views) Pirone L, Correale S, De Paola I, Zaccaro L, De Simone G, Vitagliano L, Pedone E, Di Gaetano S
Keywords: Poz Btb Domains, Protein-Protein Recognition, Structure-Function Relationships, Ubiquitination, Cullin, Protein Kctd, Unclassified Drug, Article, Molecular Model, Peptide Analysis, Peptide Synthesis, Priority Journal, Protein Binding, Protein Domain, Protein Protein Interaction, Circular Dichroism, Cullin Proteins, Enzyme-Linked Immunosorbent Assay, Humans, Potassium Channels, Protein Structure, Secondary, Poxviridae,
Affiliations: *** IBB - CNR ***
Institute of Biostructures and Bioimaging, CNR, 80134 Napoli, Italy
Department of Biological Sciences, Federico II University, 80134 Napoli, Italy
References: Not available.
Design, synthesis and characterization of a peptide able to bind proteins of the KCTD family: implications for KCTD - cullin 3 recognition
Pox virus Zinc/Bric-a-brac, Tramtrack and Broad (POZ/BTB) is a widespread domain detected in proteins involved in a variety of biological processes. Human genome analyses have unveiled the presence of POZ/BTB domain in a class of proteins (KCTD) whose role as important players in crucial biological processes is emerging. The development of new molecular entities able to interact with these proteins and to modulate their activity is a field of relevant interest. By using molecular modeling and literature mutagenesis analyses, we here designed and characterized a peptide that is able to interact with submicromolar affinities with two different members (KCTD11 and KCTD5) of this family. This finding suggests that the tetrameric KCTD11 and the pentameric KCTD5 are endowed with a similar cavity at the subunit-subunit interface deputed to the Cul3 binding, despite their different oligomeric states. Copyright (C) 2011 European Peptide Society and John Wiley & Sons, Ltd.
Design, synthesis and characterization of a peptide able to bind proteins of the KCTD family: implications for KCTD - cullin 3 recognition