VP22 core domain from herpes simplex virus 1 reveals a surprising structural conservation in both the alpha- and gammaherpesvirinae subfamilies

Journal of General Virology

Volumn 96, Issue , 2015, Pages 1436-1445

  Hew, Kelly ^a   Dahlroth, Sue Li ^a   Pan, Lucy Xin ^a   Cornvik, Tobias ^a   Nordlund, Pär ^a,b  

^a NANYANG TECHNOLOGICAL UNIVERSITY   (Singapore)

^b KAROLINSKA INSTITUTE   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; PROTEIN VP22; HERPES SIMPLEX VIRUS TYPE 1 PROTEIN VP22; VIRAL PROTEIN; VIRUS PROTEIN;

ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; DIMERIZATION; GAMMAHERPESVIRINAE; HERPES SIMPLEX VIRUS 1; HYDROGEN BOND; INTEGUMENT; LIGHT SCATTERING; MUTAGENESIS; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY; CHEMICAL STRUCTURE; CHEMISTRY; CONSERVED SEQUENCE; GENETICS; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; RHADINOVIRUS; X RAY CRYSTALLOGRAPHY;

ALPHAHERPESVIRINAE; GAMMAHERPESVIRINAE; HERPESVIRIDAE; HUMAN HERPESVIRUS 1; MIRIDAE; MURIDAE;

CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; HERPESVIRUS 1, HUMAN; MODELS, MOLECULAR; PROTEIN CONFORMATION; RHADINOVIRUS; VIRAL STRUCTURAL PROTEINS;

EID: 84937604234     PISSN: 00221317     EISSN: 14652099     Source Type: Journal    
DOI: 10.1099/vir.0.000078     Document Type: Article

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