Premium
Design, synthesis and characterization of a peptide able to bind proteins of the KCTD family: implications for KCTD—cullin 3 recognition
Author(s) -
Pirone Luciano,
Correale Stefania,
Paola Ivan de,
Zaccaro Laura,
Simone Giuseppina De,
Vitagliano Luigi,
Pedone Emilia,
Gaetano Sonia Di
Publication year - 2011
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1366
Subject(s) - cullin , peptide , mutagenesis , protein subunit , computational biology , biology , biochemistry , chemistry , microbiology and biotechnology , gene , mutation , ubiquitin , ubiquitin ligase
Pox virus Zinc/Bric‐à‐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 © 2011 European Peptide Society and John Wiley & Sons, Ltd.