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2wk5
From Proteopedia
| 2wk5, resolution 2.99Å () | |||||||||
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| Ligands: | |||||||||
| Activity: | Thymidine phosphorylase, with EC number 2.4.2.4 | ||||||||
| Related: | 2j0f, 1uou, 2wk6 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
STRUCTURAL FEATURES OF NATIVE HUMAN THYMIDINE PHOSPHORYLASE AND IN COMPLEX WITH 5-IODOURACIL
Thymidine phosphorylase (TP) first identified as platelet derived endothelial cell growth factor (PD-ECGF) plays a key role in nucleoside metabolism. Human TP (hTP) is implicated in angiogenesis and is overexpressed in several solid tumors. Here, we report the crystal structures of recombinant hTP and its complex with a substrate 5-iodouracil (5IUR) at 3.0 and 2.5A, respectively. In addition, we provide information on the role of specific residues in the enzymatic activity of hTP through mutagenesis and kinetic studies.
Structures of native human thymidine phosphorylase and in complex with 5-iodouracil., Mitsiki E, Papageorgiou AC, Iyer S, Thiyagarajan N, Prior SH, Sleep D, Finnis C, Acharya KR, Biochem Biophys Res Commun. 2009 Sep 4;386(4):666-70. Epub 2009 Jun 23. PMID:19555658
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2wk5 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Mitsiki E, Papageorgiou AC, Iyer S, Thiyagarajan N, Prior SH, Sleep D, Finnis C, Acharya KR. Structures of native human thymidine phosphorylase and in complex with 5-iodouracil. Biochem Biophys Res Commun. 2009 Sep 4;386(4):666-70. Epub 2009 Jun 23. PMID:19555658 doi:10.1016/j.bbrc.2009.06.104
Categories: Homo sapiens | Thymidine phosphorylase | Acharya, K R. | Finnis, C. | Iyer, S. | Mitsiki, E. | Papageorgiou, A C. | Prior, S H. | Sleep, D. | Thiyagarajan, N. | 5-iodouracil | Angiogenesis | Chemotaxis | Developmental protein | Differentiation | Disease mutation | Enzyme kinetic | Glycosyltransferase | Growth factor | Mutagenesis | Transferase
