Solution structure of the cGMP binding GAF domain from phosphodiesterase 5: Insights into nucleotide specificity, dimerization, and cGMP-dependent conformational change

Journal of Biological Chemistry

Volumn 283, Issue 33, 2008, Pages 22749-22759

  Heikaus, Clemens C ^a   Stout, Joseph R ^a   Sekharan, Monica R ^a,b   Eakin, Catherine M ^a   Rajagopal, Ponni ^a   Brzovic, Peter S ^a   Beavo, Joseph A ^a   Klevit, Rachel E ^a  

^a UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

^b RUTGERS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; DIMERIZATION; FETAL MONITORING; HYDROGEN; HYDROGEN BONDS; LAWS AND LEGISLATION; MACHINE DESIGN; NUCLEAR MAGNETIC RESONANCE; NUCLEIC ACIDS; PORT TERMINALS;

ADENYLYL CYCLASE; ALANINE MUTATIONS; BINDING POCKETS; CATALYTIC DOMAINS; CONFORMATIONAL CHANGES; DO-MAINS; GUANINE RINGS; HYDROLYTIC ACTIVITIES; INTRACELLULAR LEVELS; LIGAND BINDINGS; NUCLEOTIDE BINDINGS; OVERHAUSER EFFECTS; PHOSPHODIESTERASE; REGULATORY DOMAINS; REGULATORY MECHANISMS; SOLUTION STRUCTURES; STRUCTURAL BASES; STRUCTURAL CONFORMATIONS;

NUCLEOTIDES;

ADENYLATE CYCLASE; ADENYLYL CYCLASE CYAB2; ALANINE; ASPARTIC ACID; CYCLIC GMP; PHOSPHODIESTERASE; PHOSPHODIESTERASE 2A; PHOSPHODIESTERASE V; UNCLASSIFIED DRUG; PDE5A PROTEIN, HUMAN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; BINDING AFFINITY; CONFORMATIONAL TRANSITION; DIMERIZATION; ENZYME CONFORMATION; GAF DOMAIN; NUCLEAR OVERHAUSER EFFECT; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; HUMAN; KINETICS; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION;

BINDING SITES; CYCLIC GMP; CYCLIC NUCLEOTIDE PHOSPHODIESTERASES, TYPE 5; DIMERIZATION; HUMANS; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

EID: 53049094120     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M801577200     Document Type: Article

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