Functional and crystal structure analysis of active site adaptations of a potent anti-angiogenic human tRNA synthetase.

Yang, Xiang-Lei; Guo, Min; Kapoor, Mili; Ewalt, Karla L; Otero, Francella J; Skene, Robert J; McRee, Duncan E; Schimmel, Paul

Yang, Xiang-Lei; Guo, Min; Kapoor, Mili; Ewalt, Karla L; Otero, Francella J; Skene, Robert J; McRee, Duncan E; Schimmel, Paul.

Affiliation

Yang XL; The Scripps Research Institute, BCC-379, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. xlyang@scripps.edu

Structure ; 15(7): 793-805, 2007 Jul.

Article in En | MEDLINE | ID: mdl-17637340

Subject(s)

Angiogenesis Inhibitors/chemistry; Models, Molecular; Protein Folding; Tryptophan-tRNA Ligase/chemistry; Acetylation; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Binding Sites; Crystallography, X-Ray; Geobacillus stearothermophilus/metabolism; Humans; Molecular Sequence Data; Mutation; Protein Structure, Tertiary; RNA Splicing; Substrate Specificity; Tryptophan-tRNA Ligase/genetics

Fulltext

Add to My VHL

XML

PubMed Links

Search on Google

Full text: 1 Database: MEDLINE Main subject: Tryptophan-tRNA Ligase / Models, Molecular / Protein Folding / Angiogenesis Inhibitors Type of study: Prognostic_studies Limits: Humans Language: En Journal: Structure Journal subject: BIOLOGIA MOLECULAR / BIOQUIMICA / BIOTECNOLOGIA Year: 2007 Type: Article Affiliation country: United States

Fulltext

Add to My VHL

XML

PubMed Links

Search on Google