The structure of a human p110α/p85α complex elucidates the effects of oncogenic PI3Kα mutations

Science

Volumn 318, Issue 5857, 2007, Pages 1744-1748

  Huang, Chuan Hsiang ^a   Mandelker, Diana ^b   Schmidt Kittler, Oleg ^b   Samuels, Yardena ^b,c   Velculescu, Victor E ^b   Kinzler, Kenneth W ^b   Vogelstein, Bert ^b   Gabelli, Sandra B ^b   Amzel, L Mario ^b  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b JOHNS HOPKINS UNIVERSITY   (United States)

^c NATIONAL HUMAN GENOME RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; PROTEIN P110; PROTEIN P110 ALPHA; PROTEIN P85; PROTEIN P85 ALPHA; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATE; PHOSPHATIDYLINOSITOL 3 KINASE; PIK3CA PROTEIN, HUMAN; PROTEIN SUBUNIT;

CATALYSIS; ENZYME ACTIVITY; GENE; MUTATION; PEPTIDE; TUMOR;

ALPHA CHAIN; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CATALYST; COMPLEX FORMATION; DNA MODIFICATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME REGULATION; ENZYME STRUCTURE; ENZYME SUBUNIT; GENE MUTATION; HUMAN; MUTATION RATE; ONCOGENE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; NEOPLASM; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SRC HOMOLOGY DOMAIN; X RAY CRYSTALLOGRAPHY;

1-PHOSPHATIDYLINOSITOL 3-KINASE; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NEOPLASMS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; SRC HOMOLOGY DOMAINS;

EID: 37249056471     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1150799     Document Type: Article

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59. Support was provided by the Virginia and D. K. Ludwig Fund for Cancer Research. NIH grants CA 43460 to B.V., GM066895 to L.M.A, and GM07309 and GM 07184 to D.M. Brookhaven National Laboratory is gratefully acknowledged for providing Beamlines X29 and X6a of the National Synchrotron Light Source for collection of the diffraction data. We are grateful to Jr-Ming Yang for the identification of the crystallization condition. Coordinates of the p110a/niSH2 have been deposited in the Protein Data Bank (accession number 2RD0, www.rcsb.org).