Structure of serum amyloid A suggests a mechanism for selective lipoprotein binding and functions: SAA as a hub in macromolecular interaction networks

FEBS Letters

Volumn 590, Issue 6, 2016, Pages 866-879

  Frame, Nicholas M ^a   Gursky, Olga ^a  

^a BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

acute phase high density lipoprotein; amino acid sequence and structural analyses; immune response and reactive AA amyloidosis; intrinsically disordered protein hub; reverse cholesterol transport and atherosclerosis

Indexed keywords

APOLIPOPROTEIN A1; APOLIPOPROTEIN A4; APOLIPOPROTEIN E; HIGH DENSITY LIPOPROTEIN; LIPOPROTEIN; PROTEOGLYCAN; SERUM AMYLOID A; LIGAND; MULTIPROTEIN COMPLEX; PROTEIN BINDING;

ALPHA HELIX; AMINO ACID SEQUENCE; AMYLOIDOSIS; ARTICLE; BINDING AFFINITY; BINDING KINETICS; BINDING SITE; BIOINFORMATICS; C DOMAIN; CHOLESTEROL TRANSPORT; CONTROLLED STUDY; CRYSTAL STRUCTURE; HYDROPHOBICITY; IMMUNE RESPONSE; LIGAND BINDING; LIPID HOMEOSTASIS; MACROMOLECULAR INTERACTION NETWORK; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; N DOMAIN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CLEAVAGE; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; SELECTIVE LIPOPROTEIN BINDING; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; STRUCTURE ACTIVITY RELATION; SURFACE PROPERTY; ANIMAL; CHEMICAL PHENOMENA; CHEMISTRY; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; MOLECULAR MODEL; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; AMYLOIDOSIS; ANIMALS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; LIGANDS; LIPOPROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIPROTEIN COMPLEXES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN INTERACTION MAPS; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; SERUM AMYLOID A PROTEIN;

EID: 84960171624     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1002/1873-3468.12116     Document Type: Article

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