Interfacial residues promote an optimal alignment of the catalytic center in human soluble guanylate cyclase: Heterodimerization is required but not sufficient for activity

Biochemistry

Volumn 53, Issue 13, 2014, Pages 2153-2165

  Seeger, Franziska ^a,c   Quintyn, Royston ^b   Tanimoto, Akiko ^b   Williams, Gareth J ^c   Tainer, John A ^c,d   Wysocki, Vicki H ^b   Garcin, Elsa D ^a  

^a UNIVERSITY OF MARYLAND BALTIMORE COUNTY   (United States)

^b OHIO STATE UNIVERSITY   (United States)

^c LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^d SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARDIOVASCULAR SYSTEM; HYDROGEN BONDS; MASS SPECTROMETRY; X RAY CRYSTALLOGRAPHY;

ACTIVITY MEASUREMENTS; DOMAIN INTERACTIONS; HYDROGEN BOND NETWORKS; NATIVE MASS SPECTROMETRIES; PULMONARY HYPERTENSION; REGULATORY MECHANISM; SOLUBLE GUANYLATE CYCLASE (SGC); THREE-DIMENSIONAL STRUCTURE;

CONFORMATIONS;

GUANYLATE CYCLASE; HEME; HETERODIMER;

ARTICLE; DIMERIZATION; ENZYME ACTIVITY; ENZYME MECHANISM; HUMAN; HYDROGEN BOND; MASS SPECTROMETRY; MOLECULAR DOCKING; PRIORITY JOURNAL; SIGNAL TRANSDUCTION; X RAY CRYSTALLOGRAPHY;

BIOCATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; GUANYLATE CYCLASE; HUMANS; HYDROGEN BONDING; MASS SPECTROMETRY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN MULTIMERIZATION; RECEPTORS, CYTOPLASMIC AND NUCLEAR;

EID: 84898052397     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500129k     Document Type: Article

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