The structure of S100A11 fragment explains a local structural change induced by phosphorylation

Journal of Peptide Science

Volumn 14, Issue 10, 2008, Pages 1129-1138

  Kouno, Takahide ^a   Mizuguchi, Mineyuki ^a   Sakaguchi, Masakiyo ^b   Makino, Eiichi ^b   Mori, Yoshihiro ^a   Shinoda, Hiroyuki ^a   Aizawa, Tomoyasu ^c   Demura, Makoto ^c   Huh, Nam Ho ^b   Kawano, Keiichi ^c  

^a UNIVERSITY OF TOYAMA   (Japan)

^b OKAYAMA UNIVERSITY   (Japan)

^c HOKKAIDO UNIVERSITY   (Japan)

Author keywords

Keratinocyte; MAK19 peptide; Phosphorylation; S100A11; Solution structure; Trifluorethanol

Indexed keywords

METHIONYLALANYLLYSYLISOLEUCYLSERYLSERYLPROLYLTHREONYLGLUTAMYLTHREONYLGLUTAMYLARGINYLCYSTEINYLISOLEUCYLGLUTAMYLSERYLLEUCYLISOLEUCYLALANINE; NUCLEOLIN; POLYPEPTIDE; PROTEIN S 100; PROTEIN S 100A11; THREONINE; TRIFLUOROETHANOL; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; DIMERIZATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PHOSPHORYLATION; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; CELL DIFFERENTIATION; DIMERIZATION; EF HAND MOTIFS; HUMANS; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PHOSPHOPROTEINS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN TRANSPORT; RNA-BINDING PROTEINS; S100 PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 57849094493     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1050     Document Type: Article

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