Structural basis of the recognition of the samp motif of adenomatous polyposis coli by the src-homology 3 domain

Biochemistry

Volumn 49, Issue 25, 2010, Pages 5143-5153

  Kaieda, Shuji ^a   Matsui, Chiyuki ^b   Mimori Kiyosue, Yuko ^c   Ikegami, Takahisa ^a  

^a OSAKA UNIVERSITY   (Japan)

^b KAN Research Institute Inc ^*  (Japan)

^c RIKEN Center for Biosystems Dynamics Research   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOMATOUS POLYPOSIS COLI; BACKBONE DYNAMICS; BIOLOGICAL MOLECULE; CLASS II; COMPLEX STRUCTURE; CONVENTIONAL METHODS; FREE STATE; FUSION PROTEINS; HIGH FLEXIBILITY; HIGH SELECTIVITY; HYDROPHOBIC POCKETS; INTERACTION NETWORKS; LIVING SYSTEMS; LOCAL MOTIONS; NORMAL FUNCTION; PEPTIDE RECOGNITION; POLYPEPTIDE CHAIN; POLYPROLINE; RECOGNITION SEQUENCE; SEQUENCE MOTIFS; SOLUTION STRUCTURES; SPIN RELAXATION; SRC-HOMOLOGY; STABLE COMPLEXES; STRUCTURAL BASIS; TUMOR SUPPRESSION; TUMOR SUPPRESSORS; TYPE II;

SPIN DYNAMICS; TUMORS;

PROTEINS;

APC PROTEIN; CARRIER PROTEIN; MEMBRANE PROTEIN; PROTEIN DDEF1; PROTEIN SAMP; PROTEIN SH3; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN STRUCTURE;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; GENES, APC; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; SRC HOMOLOGY DOMAINS;

EID: 77953901791     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100563z     Document Type: Article

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