The acidic domain of hnRNPQ (NSAP1) has structural similarity to Barstar and binds to Apobec1

Biochemical and Biophysical Research Communications

Volumn 350, Issue 2, 2006, Pages 288-297

  Quaresma, Alexandre J C ^a,b   Oyama Jr , Sergio ^a   Barbosa, João A R G ^a,b   Kobarg, Jörg ^a,b  

^a LABORATÓRIO NACIONAL DE LUZ SÍNCROTRON   (Brazil)

^b UNIVERSITY OF CAMPINAS   (Brazil)

Author keywords

AcD domain; Apobec1; Circular dichroism; hnRNPQ NSAP1; Molecular dynamics; Molecular modeling; Protein protein interactions; RNA editing

Indexed keywords

APOB EDITING CATALYTIC SUBUNIT 1; BACTERIAL PROTEIN; HETEROGENOUS NUCLEAR RIBONUCLEOPROTEIN Q; NON STRUCTURAL ASSOCIATED PROTEIN 1; PROTEIN BARSTAR; PROTEIN SUBUNIT; RIBONUCLEOPROTEIN; UNCLASSIFIED DRUG;

ARTICLE; COMPUTER MODEL; IN VITRO STUDY; MOLECULAR DYNAMICS; MOLECULAR MODEL; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CIRCULAR DICHROISM; COMPUTER SIMULATION; CYTIDINE DEAMINASE; HETEROGENEOUS-NUCLEAR RIBONUCLEOPROTEINS; HISTIDINE; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; PROTEIN KINASE C; PROTEIN STRUCTURE, TERTIARY; RNA-BINDING PROTEINS; SEQUENCE ALIGNMENT; SERINE; SPECTROMETRY, FLUORESCENCE; STRUCTURAL HOMOLOGY, PROTEIN;

BACTERIA (MICROORGANISMS);

EID: 33749322939     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.09.044     Document Type: Article

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