Allosteric signal transmission involves synergy between discrete structural units of the regulatory subunit of aspartate transcarbamoylase

Archives of Biochemistry and Biophysics

Volumn 373, Issue 2, 2000, Pages 352-360

  Liu, Leyuan ^a   Wales, Melinda E ^a   Wild, James R ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

Author keywords

Allosteric zinc interface; Allosterism; ATCase; Ligand binding; Mutational effect; S5' strand; Signal transmission

Indexed keywords

ADENOSINE TRIPHOSPHATE; ASPARTATE CARBAMOYLTRANSFERASE; CYTIDINE TRIPHOSPHATE; POLYPEPTIDE; ZINC;

ALLOSTERISM; ARTICLE; CHIMERA; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; SIGNAL TRANSDUCTION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; SERRATIA MARCESCENS;

EID: 0034650362     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1006/abbi.1999.1570     Document Type: Article

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