Structural basis for recognition of acidic-cluster dileucine sequence by GGA1

Nature

Volumn 415, Issue 6874, 2002, Pages 937-941

  Shiba, Tomoo ^a,b   Takatsu, Hiroyuki ^c   Nogi, Terukazu ^a   Matsugaki, Naohiro ^a   Kawasaki, Masato ^a   Igarashi, Noriyuki ^a   Suzuki, Mamoru ^a   Kato, Ryuichi ^a   Earnest, Thomas ^d   Nakayama, Kazuhisa ^c   Wakatsuki, Soichi ^a  

^a HIGH ENERGY ACCELERATOR RESEARCH ORGANIZATION KEK   (Japan)

^b Foundation for Advancement of International Science   (Japan)

^c UNIVERSITY OF TSUKUBA   (Japan)

^d LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROPHOBICITY; POSITIVE IONS; X RAY ANALYSIS;

HOMOLOGY; PEPTIDES;

PROTEINS;

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; BINDING PROTEIN; CLATHRIN; GOLGI LOCALIZING GAMMA ADAPTIN EAR HOMOLOGY DOMAIN ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR INTERACTING PROTEIN; LEUCINE; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; PROTEIN; PROTEIN HRS; PROTEIN TOM1; PROTEIN VHS; SOMATOMEDIN B RECEPTOR; SORTILIN; UNCLASSIFIED DRUG;

BIOCHEMISTRY; PROTEIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; ELECTRICITY; ENDOSOME; HYDROPHOBICITY; LYSOSOME; MOLECULAR MECHANICS; MOLECULAR RECOGNITION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; TRANS GOLGI NETWORK; X RAY ANALYSIS;

ADAPTOR PROTEINS, VESICULAR TRANSPORT; ADP-RIBOSYLATION FACTORS; AMINO ACID SEQUENCE; BINDING SITES; CARRIER PROTEINS; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; LEUCINE; MEMBRANE GLYCOPROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; RECEPTOR, IGF TYPE 2; STRUCTURE-ACTIVITY RELATIONSHIP; TWO-HYBRID SYSTEM TECHNIQUES;

EID: 18244400470     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/415937a     Document Type: Article

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