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[Evolutionary trace analysis of N-myristoyltransferase family].
- Source :
-
Yao xue xue bao = Acta pharmaceutica Sinica [Yao Xue Xue Bao] 2007 Feb; Vol. 42 (2), pp. 157-65. - Publication Year :
- 2007
-
Abstract
- To clarify the important functional residues in the active site of N-myristoyltransferase (NMT), a novel antifungal drug target, and to guide the design of specific inhibitors, multiple sequence alignments were performed on the NMT family and thus evolutionary trace was constructed. The important functional residues in myristoyl CoA binding site, catalytic center and inhibitor binding site of NMT family were identified by ET analysis. The trace residues were mapped onto the active site of CaNMT. Trpl26, Asn175 and Thr211 are highly conserved trace residues and do not interact with current NMT inhibitors, which are potential novel drug binding sites for the novel inhibitor design. Pro338, Leu350, Ile352 and Ala353 are class-specific trace residues, which are important for the optimization of current NMT inhibitors. The trace residues identified by ET analysis are of great importance to study the structure-function relationship and also to guide the design of specific inhibitors.
- Subjects :
- Acyltransferases chemistry
Amino Acid Sequence
Animals
Binding Sites
Conserved Sequence
Enzyme Inhibitors chemistry
Enzyme Inhibitors pharmacology
Evolution, Molecular
Humans
Imidazoles chemistry
Imidazoles pharmacology
Models, Molecular
Molecular Sequence Data
Oligopeptides chemistry
Oligopeptides pharmacology
Phylogeny
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Acyl Coenzyme A metabolism
Acyltransferases genetics
Acyltransferases metabolism
Subjects
Details
- Language :
- Chinese
- ISSN :
- 0513-4870
- Volume :
- 42
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Yao xue xue bao = Acta pharmaceutica Sinica
- Publication Type :
- Academic Journal
- Accession number :
- 17518043