Design, synthesis and characterization of a peptide able to bind proteins of the KCTD family: implications for KCTD—cullin 3 recognition
✍ Scribed by Luciano Pirone; Stefania Correale; Ivan de Paola; Laura Zaccaro; Giuseppina De Simone; Luigi Vitagliano; Emilia Pedone; Sonia Di Gaetano
- Publisher
- John Wiley and Sons
- Year
- 2011
- Tongue
- English
- Weight
- 138 KB
- Volume
- 17
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.1366
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
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.