Structure of transmembrane domain of lysosome-associated membrane protein type 2a (LAMP-2A) reveals key features for substrate specificity in chaperone-mediated autophagy

Journal of Biological Chemistry

Volumn 289, Issue 51, 2014, Pages 35111-35123

  Rout, Ashok K ^a   Strub, Marie Paule ^a   Piszczek, Grzegorz ^a   Tjandra, Nico ^a  

^a NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BIOLOGICAL MEMBRANES; NUCLEAR MAGNETIC RESONANCE; SUBSTRATES;

CHAPERONE-MEDIATED AUTOPHAGY; NUCLEAR MAGNETIC RESONANCE(NMR); PROTEIN TRANSLOCATION; STRUCTURE AND DYNAMICS; SUBSTRATE RECOGNITION; SUBSTRATE SPECIFICITY; TRANS-MEMBRANE DOMAINS; TRANS-MEMBRANE PROTEINS;

PROTEINS;

CHAPERONE; DODECYLPHOSPHORYLCHOLINE; HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN 40; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2A; MEMBRANE PROTEIN; PEPTIDE; PROTEIN; RIBONUCLEASE A; UNCLASSIFIED DRUG; LAMP2 PROTEIN, HUMAN; MICELLE; PHOSPHORYLCHOLINE; PROTEIN BINDING;

ARTICLE; AUTOPHAGY; BINDING AFFINITY; CELL ENERGY; CELL STRESS; CONTROLLED STUDY; CYTOSOL; ENZYME SPECIFICITY; LYSOSOME; LYSOSOME MEMBRANE; MOLECULAR INTERACTION; MOLECULAR RECOGNITION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN METABOLISM; PROTEIN TRANSPORT; AMINO ACID SEQUENCE; ANALOGS AND DERIVATIVES; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HUMAN; KINETICS; METABOLISM; MICELLE; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROCEDURES; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SEQUENCE; AUTOPHAGY; HSC70 HEAT-SHOCK PROTEINS; HUMANS; KINETICS; LYSOSOMAL-ASSOCIATED MEMBRANE PROTEIN 2; MAGNETIC RESONANCE SPECTROSCOPY; MICELLES; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PHOSPHORYLCHOLINE; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY;

EID: 84919488445     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.609446     Document Type: Article

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