APOBEC2 is a monomer in solution: Implications for APOBEC3G Models

Biochemistry

Volumn 51, Issue 9, 2012, Pages 2008-2017

  Krzysiak, Troy C ^a   Jung, Jinwon ^a   Thompson, James ^b   Baker, David ^b   Gronenborn, Angela M ^a  

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

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

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATION PROPENSITY; ANTI-HIV ACTIVITY; DIMER INTERFACE; FULL-LENGTH PROTEINS; INTERMOLECULAR CONTACTS; N-TERMINALS; QUATERNARY STRUCTURE; SOLUTION STRUCTURES;

DIMERS; MONOMERS; PRECIPITATION (CHEMICAL); PROTEINS;

CRYSTAL STRUCTURE;

APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; APOLIPOPROTEIN B MRNA EDITING CATALYTIC POLYPEPTIDE LIKE 2; HYDROLASE; MONOMER; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN QUATERNARY STRUCTURE;

AMINO ACID SEQUENCE; CYTIDINE DEAMINASE; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; SEQUENCE ALIGNMENT; SOLUTIONS;

EID: 84863405448     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300021s     Document Type: Article

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