The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction

PLoS ONE

Volumn 6, Issue 10, 2011, Pages

  Garcia Mayoral, M Flor ^a   Castaño, Raquel ^b   Fanarraga, Monica L ^b   Zabala, Juan Carlos ^b   Rico, Manuel ^a   Bruix, Marta ^a  

^a INSTITUTO DE QUÍMICA FÍSICA ROCASOLANO   (Spain)

^b UNIVERSITY OF CANTABRIA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TUBULIN; BETA TUBULIN; BINDING PROTEIN; MESSENGER RNA; MONOMER; SPECTRIN; TUBULIN; TUBULIN BINDING COFACTOR C; UNCLASSIFIED DRUG; CHAPERONE; TUBULIN SPECIFIC CHAPERONE C; TUBULIN-SPECIFIC CHAPERONE C;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; APOPTOSIS; ARTICLE; CARBOXY TERMINAL SEQUENCE; CENTROSOME; CONTROLLED STUDY; FEMALE; GENE; GENE EXPRESSION REGULATION; HUMAN; HUMAN CELL; MITOSIS SPINDLE; MOLECULAR DYNAMICS; MOLECULAR MODEL; MOLECULAR RECOGNITION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE SEQUENCE; PROTEIN DEPLETION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; SURFACE CHARGE; TUBULIN BINDING COFACTOR C GENE; CHEMICAL STRUCTURE; CHEMISTRY; HELA CELL; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SOLUTION AND SOLUBILITY;

CENTROSOME; HELA CELLS; HUMANS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SOLUTIONS; TUBULIN;

EID: 80054738923     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025912     Document Type: Article

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