5x6t

Publication Abstract from PubMed

Synaptotagmin-like protein 4 (Slp4), expressed in human platelets, is associated with dense granule release. Slp4 is comprised of the N-terminal zinc finger, Slp homology domain, and C2 domains. We synthesized a compact construct (the Slp4N peptide) corresponding to the Slp4 N-terminal zinc finger. Herein, we have determined the solution structure of the Slp4N peptide by NMR. Furthermore, experimental, chemical modification of Cys residues revealed that the Slp4N peptide binds two zinc atoms to mediate proper folding. NMR data showed that eight Cys residues coordinate zinc atoms in a cross-brace fashion. The SMART database predicted the structure of Slp4N as a RING finger. However, the actual structure of the Slp4N peptide adopts a unique C4 C4 -type FYVE fold and is distinct from a RING fold. To create an artificial RING finger (ARF) with specific ubiquitin-conjugating enzyme (E2)-binding capability, cross-brace structures with eight zinc-ligating residues are needed as the scaffold. The cross-brace structure of the Slp4N peptide could be utilized as the scaffold for the design of ARFs. This article is protected by copyright. All rights reserved.

The unique N-terminal zinc finger of Synaptotagmin-like protein 4 reveals FYVE structure.,Miyamoto K, Nakatani A, Saito K Protein Sci. 2017 Sep 14. doi: 10.1002/pro.3301. PMID:28906046^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.