The structure of the complex of calmodulin with KAR-2: A novel mode of binding explains the unique pharmacology of the drug

Journal of Biological Chemistry

Volumn 280, Issue 9, 2005, Pages 8266-8274

  Horváth, István ^a   Harmat, Veronika ^b   Perczel, András ^b   Pálfi, Villo ^b   Nyitray, László ^b   Nagy, Attila ^b   Hlavanda, Emma ^b   Náray Szabó, Gábor ^b   Ovádi, Judit ^a  

^a INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^b EÖTVÖS LORÁND UNIVERSITY   (Hungary)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; CELLS; CONFORMATIONS; CRYSTAL STRUCTURE; CRYSTALLIZATION; CYTOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHARMACOKINETICS; PHYSIOLOGY; PROTEINS; TUMORS; X RAY DIFFRACTION ANALYSIS;

ANTAGONISTIC EFFECTS; CALMODULIN; CANCER CELLS; MITOSIS;

DRUG PRODUCTS;

3' (BETA CHLOROETHYL) 2',4' DIOXO 3,5' SPIROOXAZOLIDINO 4 DEACETOXYVINBLASTINE; AMINO ACID; ANTIMITOTIC AGENT; CALCIUM ION; CALMODULIN; NITROGEN 15; PROTON; TRIFLUOPERAZINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING KINETICS; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DRUG EFFECT; DRUG PROTEIN BINDING; DRUG STRUCTURE; DRUG TARGETING; ISOTOPE LABELING; MICROTUBULE; MITOSIS INHIBITION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; STRUCTURE ANALYSIS; THREE DIMENSIONAL IMAGING; X RAY DIFFRACTION;

ANIMALS; BINDING SITES; BRAIN; CALMODULIN; CATTLE; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; DOPAMINE ANTAGONISTS; DOSE-RESPONSE RELATIONSHIP, DRUG; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, BIOLOGICAL; MODELS, CHEMICAL; MODELS, MOLECULAR; PHOSPHORIC DIESTER HYDROLASES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP; SURFACE PLASMON RESONANCE; TIME FACTORS; TRIFLUOPERAZINE; VINBLASTINE; X-RAY DIFFRACTION;

EID: 14844324990     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M410353200     Document Type: Article

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