Crystal structure of Thermoanaerobacter tengcongensis hypoxanthine‐guanine phosphoribosyl transferase L160I mutant − insights into inhibitor design
Hypoxanthine‐guanine phosphoribosyltransferase (HGPRT) is a potential target for structure‐based inhibitor design for the treatment of parasitic diseases. We created point mutants of Thermoanaerobacter tengcongensis HGPRT and tested their activities to identify side chains that were important for fu...
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| Published in | The FEBS journal Vol. 274; no. 17; pp. 4408 - 4415 |
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| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Oxford, UK
Blackwell Publishing Ltd
01.09.2007
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| Subjects | |
| Online Access | Get full text |
| ISSN | 1742-464X 1742-4658 |
| DOI | 10.1111/j.1742-4658.2007.05970.x |
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| Abstract | Hypoxanthine‐guanine phosphoribosyltransferase (HGPRT) is a potential target for structure‐based inhibitor design for the treatment of parasitic diseases. We created point mutants of Thermoanaerobacter tengcongensis HGPRT and tested their activities to identify side chains that were important for function. Mutating residues Leu160 and Lys133 substantially diminished the activity of HGPRT, confirming their importance in catalysis. All 11 HGPRT mutants were subject to crystallization screening. The crystal structure of one mutant, L160I, was determined at 1.7 Å resolution. Surprisingly, the active site is occupied by a peptide from the N‐terminus of a neighboring tetramer. These crystal contacts suggest an alternate strategy for structure‐based inhibitor design. |
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| AbstractList | Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) is a potential target for structure-based inhibitor design for the treatment of parasitic diseases. We created point mutants of Thermoanaerobacter tengcongensis HGPRT and tested their activities to identify side chains that were important for function. Mutating residues Leu160 and Lys133 substantially diminished the activity of HGPRT, confirming their importance in catalysis. All 11 HGPRT mutants were subject to crystallization screening. The crystal structure of one mutant, L160I, was determined at 1.7 A resolution. Surprisingly, the active site is occupied by a peptide from the N-terminus of a neighboring tetramer. These crystal contacts suggest an alternate strategy for structure-based inhibitor design. Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) is a potential target for structure-based inhibitor design for the treatment of parasitic diseases. We created point mutants of Thermoanaerobacter tengcongensis HGPRT and tested their activities to identify side chains that were important for function. Mutating residues Leu160 and Lys133 substantially diminished the activity of HGPRT, confirming their importance in catalysis. All 11 HGPRT mutants were subject to crystallization screening. The crystal structure of one mutant, L160I, was determined at 1.7 A resolution. Surprisingly, the active site is occupied by a peptide from the N-terminus of a neighboring tetramer. These crystal contacts suggest an alternate strategy for structure-based inhibitor design.Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) is a potential target for structure-based inhibitor design for the treatment of parasitic diseases. We created point mutants of Thermoanaerobacter tengcongensis HGPRT and tested their activities to identify side chains that were important for function. Mutating residues Leu160 and Lys133 substantially diminished the activity of HGPRT, confirming their importance in catalysis. All 11 HGPRT mutants were subject to crystallization screening. The crystal structure of one mutant, L160I, was determined at 1.7 A resolution. Surprisingly, the active site is occupied by a peptide from the N-terminus of a neighboring tetramer. These crystal contacts suggest an alternate strategy for structure-based inhibitor design. Hypoxanthine‐guanine phosphoribosyltransferase (HGPRT) is a potential target for structure‐based inhibitor design for the treatment of parasitic diseases. We created point mutants of Thermoanaerobacter tengcongensis HGPRT and tested their activities to identify side chains that were important for function. Mutating residues Leu160 and Lys133 substantially diminished the activity of HGPRT, confirming their importance in catalysis. All 11 HGPRT mutants were subject to crystallization screening. The crystal structure of one mutant, L160I, was determined at 1.7 Å resolution. Surprisingly, the active site is occupied by a peptide from the N‐terminus of a neighboring tetramer. These crystal contacts suggest an alternate strategy for structure‐based inhibitor design. Hypoxanthine‐guanine phosphoribosyltransferase (HGPRT) is a potential target for structure‐based inhibitor design for the treatment of parasitic diseases. We created point mutants of Thermoanaerobacter tengcongensis HGPRT and tested their activities to identify side chains that were important for function. Mutating residues Leu160 and Lys133 substantially diminished the activity of HGPRT, confirming their importance in catalysis. All 11 HGPRT mutants were subject to crystallization screening. The crystal structure of one mutant, L160I, was determined at 1.7 Å resolution. Surprisingly, the active site is occupied by a peptide from the N‐terminus of a neighboring tetramer. These crystal contacts suggest an alternate strategy for structure‐based inhibitor design. Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) is a potential target for structure-based inhibitor design for the treatment of parasitic diseases. We created point mutants of Thermoanaerobacter tengcongensis HGPRT and tested their activities to identify side chains that were important for function. Mutating residues Leu160 and Lys133 substantially diminished the activity of HGPRT, confirming their importance in catalysis. All 11 HGPRT mutants were subject to crystallization screening. The crystal structure of one mutant, L160I, was determined at 1.7 angstrom resolution. Surprisingly, the active site is occupied by a peptide from the N-terminus of a neighboring tetramer. These crystal contacts suggest an alternate strategy for structure-based inhibitor design. [PUBLICATION ABSTRACT] |
| Author | Liang, Yuhe You, Delin Chen, Qiang Luo, Ming Zheng, Xiaofeng Gu, Xiaocheng Su, Xiaodong |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/17662107$$D View this record in MEDLINE/PubMed |
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| Snippet | Hypoxanthine‐guanine phosphoribosyltransferase (HGPRT) is a potential target for structure‐based inhibitor design for the treatment of parasitic diseases. We... Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) is a potential target for structure-based inhibitor design for the treatment of parasitic diseases. We... |
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| SubjectTerms | Biochemistry Crystal structure Crystallography, X-Ray enzymatic activity Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology Enzymes HGPRT Hypoxanthine Phosphoribosyltransferase - antagonists & inhibitors Hypoxanthine Phosphoribosyltransferase - chemistry Hypoxanthine Phosphoribosyltransferase - isolation & purification Inhibitor drugs Models, Molecular mutant Mutation Protein Conformation Thermoanaerobacter - enzymology Thermoanaerobacter tengcongensis |
| Title | Crystal structure of Thermoanaerobacter tengcongensis hypoxanthine‐guanine phosphoribosyl transferase L160I mutant − insights into inhibitor design |
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