Structural features of human inositol phosphate multikinase rationalize its inositol phosphate kinase and phosphoinositide 3-kinase activities. [electronic resource]
Producer: 20171121Description: 18192-18202 p. digitalISSN:- 1083-351X
- Amino Acid Sequence
- Amino Acid Substitution
- Binding Sites
- Carbohydrate Conformation
- Catalytic Domain
- Conserved Sequence
- Crystallography, X-Ray
- Humans
- Inositol 1,4,5-Trisphosphate -- chemistry
- Inositol Phosphates -- chemistry
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Phosphotransferases (Alcohol Group Acceptor) -- chemistry
- Protein Conformation
- Protein Interaction Domains and Motifs
- Protein Structure, Secondary
- Recombinant Proteins -- chemistry
- Sequence Alignment
- Substrate Specificity
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Publication Type: Comparative Study; Journal Article; Research Support, N.I.H., Intramural
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