The X-ray structure of the FMN-binding protein atHal3 provides the structural basis for the activity of a regulatory subunit involved in signal transduction

Structure

Volumn 8, Issue 9, 2000, Pages 961-969

  Albert, Armando ^a   Martínez Ripoll, Martín ^a   Espinosa Ruiz, Ana ^b   Yenush, Lynne ^b   Culiáñez Macià, Francisco A ^b   Serrano, Ramón ^b  

^a INSTITUTO DE QUÍMICA FÍSICA ROCASOLANO   (Spain)

^b Ciudad Politécnica de la Innovación   (Spain)

Author keywords

Cell growth; Flavoprotein; Protein crystallography; Regulation; Salt stress; Signal transduction

Indexed keywords

BINDING PROTEIN; FLAVINE MONONUCLEOTIDE; FLAVINE MONONUCLEOTIDE BINDING PROTEIN; FLAVOPROTEIN; GENE PRODUCT; UNCLASSIFIED DRUG;

ARABIDOPSIS; ARTICLE; NONHUMAN; OSMOTIC STRESS; PLANT GROWTH; PRIORITY JOURNAL; PROTEIN STRUCTURE; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS; TRANSGENIC PLANT; X RAY ANALYSIS;

ARABIDOPSIS; ARABIDOPSIS THALIANA; FUNGI; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE; STAPHYLOCOCCUS EPIDERMIDIS;

EID: 0034665046     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00187-8     Document Type: Article

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