Specific residues of a conserved domain in the N terminus of the human cytomegalovirus pUL50 protein determine its intranuclear interaction with pUL53

Journal of Biological Chemistry

Volumn 287, Issue 28, 2012, Pages 24004-24016

  Milbradt, Jens ^a   Auerochs, Sabrina ^a   Sevvana, Madhumati ^a   Muller, Yves A ^a   Sticht, Heinrich ^a   Marschall, Manfred ^a  

^a UNIVERSITY OF ERLANGEN NUREMBERG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMPHIPATHIC; BINDING PROPERTIES; BIOPHYSICAL ANALYSIS; CELLULAR PROTEINS; CONSERVED REGIONS; CONSERVED RESIDUES; FUNCTIONAL INTERACTION; GLOBULAR DOMAINS; HOST CELLS; HUMAN CYTOMEGALOVIRUS; IN-SILICO; INFECTED CELLS; INTRANUCLEAR INTERACTIONS; N-TERMINALS; NUCLEAR ENVELOPE; REGULAR SECONDARY STRUCTURES;

AMINO ACIDS; BINDING ENERGY; CYTOLOGY;

PROTEINS;

ALANINE; AMINO ACID DERIVATIVE; GLUTAMIC ACID; MUTANT PROTEIN; PHENYLALANINE; PROTEIN PUL50; PROTEIN PUL53; TYROSINE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BIOPHYSICS; CELL NUCLEUS MEMBRANE; COMPUTER MODEL; CONTROLLED STUDY; GENETIC CONSERVATION; HERPES VIRUS; HUMAN; HUMAN CELL; HUMAN CYTOMEGALOVIRUS; MUTATIONAL ANALYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; AMINO ACIDS; BINDING SITES; BLOTTING, WESTERN; CELL NUCLEUS; CONSERVED SEQUENCE; CYTOMEGALOVIRUS; GLUTAMIC ACID; GREEN FLUORESCENT PROTEINS; HEK293 CELLS; HELA CELLS; HUMANS; MICROSCOPY, CONFOCAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; TYROSINE; VIRAL PROTEINS;

HERPESVIRIDAE; HUMAN HERPESVIRUS 5; MIRIDAE;

EID: 84863614597     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.331207     Document Type: Article

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