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Nuclear Magnetic Resonance Structure of the Human Polyoma JC Virus Agnoprotein
Author(s) -
Coric Pascale,
Saribas A. Sami,
AbouGharbia Magid,
Childers Wayne,
Condra Jon H.,
White Martyn K.,
Safak Mahmut,
Bouaziz Serge
Publication year - 2017
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.25977
Subject(s) - helix (gastropod) , amino acid , peptide sequence , nuclear magnetic resonance spectroscopy , peptide , protein structure , chemistry , biology , biochemistry , stereochemistry , gene , ecology , snail
ABSTRACT Agnoprotein is an important regulatory protein of the human polyoma JC virus (JCV) and plays critical roles during the viral replication cycle. It forms highly stable dimers and oligomers through its Leu/Ile/Phe‐rich domain, which is important for the stability and function of the protein. We recently resolved the partial 3D structure of this protein by NMR using a synthetic peptide encompassing amino acids Thr17 to Gln52, where the Leu/Ile/Phe‐ rich region was found to adopt a major alpha‐helix conformation spanning amino acids 23–39. Here, we report the resolution of the 3D structure of full‐length JCV agnoprotein by NMR, which not only confirmed the existence of the previously reported major α‐helix domain at the same position but also revealed the presence of an additional minor α‐helix region spanning amino acid residues Leu6 to lys13. The remaining regions of the protein adopt an intrinsically unstructured conformation. J. Cell. Biochem. 118: 3268–3280, 2017. © 2017 Wiley Periodicals, Inc.