2wk6

From Proteopedia

(Difference between revisions)

Revision as of 07:52, 20 January 2015

STRUCTURAL FEATURES OF NATIVE HUMAN THYMIDINE PHOSPHORYLASE AND IN COMPLEX WITH 5-IODOURACIL

Structural highlights

2wk6 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2j0f, 2wk5, 1uou
Activity:	Thymidine phosphorylase, with EC number 2.4.2.4
Resources:	FirstGlance, OCA, RCSB, PDBsum

Disease

[TYPH_HUMAN] Mitochondrial neurogastrointestinal encephalomyopathy. The disease is caused by mutations affecting the gene represented in this entry.^[1] ^[2]

Function

[TYPH_HUMAN] May have a role in maintaining the integrity of the blood vessels. Has growth promoting activity on endothelial cells, angiogenic activity in vivo and chemotactic activity on endothelial cells in vitro.^[3] Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis.^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nishino I, Spinazzola A, Hirano M. Thymidine phosphorylase gene mutations in MNGIE, a human mitochondrial disorder. Science. 1999 Jan 29;283(5402):689-92. PMID:9924029
↑ Gamez J, Ferreiro C, Accarino ML, Guarner L, Tadesse S, Marti RA, Andreu AL, Raguer N, Cervera C, Hirano M. Phenotypic variability in a Spanish family with MNGIE. Neurology. 2002 Aug 13;59(3):455-7. PMID:12177387
↑ Usuki K, Saras J, Waltenberger J, Miyazono K, Pierce G, Thomason A, Heldin CH. Platelet-derived endothelial cell growth factor has thymidine phosphorylase activity. Biochem Biophys Res Commun. 1992 May 15;184(3):1311-6. PMID:1590793
↑ Usuki K, Saras J, Waltenberger J, Miyazono K, Pierce G, Thomason A, Heldin CH. Platelet-derived endothelial cell growth factor has thymidine phosphorylase activity. Biochem Biophys Res Commun. 1992 May 15;184(3):1311-6. PMID:1590793
↑ 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

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2wk6"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2wk6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WK6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WK6 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IUR:5-IODOURACIL'>IUR</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IUR:5-IODOURACIL'>IUR</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j0f|2j0f]], [[2wk5|2wk5]], [[1uou|1uou]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j0f|2j0f]], [[2wk5|2wk5]], [[1uou|1uou]]</td></tr>
-<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymidine_phosphorylase Thymidine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.4 2.4.2.4] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymidine_phosphorylase Thymidine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.4 2.4.2.4] </span></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wk6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wk6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wk6 RCSB], [http://www.ebi.ac.uk/pdbsum/2wk6 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wk6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wk6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wk6 RCSB], [http://www.ebi.ac.uk/pdbsum/2wk6 PDBsum]</span></td></tr>
-<table>
+</table>
 == Disease ==
 [[http://www.uniprot.org/uniprot/TYPH_HUMAN TYPH_HUMAN]] Mitochondrial neurogastrointestinal encephalomyopathy. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:9924029</ref> <ref>PMID:12177387</ref>
@@ Line 36: / Line 36: @@
 [[Category: Homo sapiens]]
 [[Category: Thymidine phosphorylase]]
-[[Category: Acharya, K R.]]
+[[Category: Acharya, K R]]
-[[Category: Finnis, C.]]
+[[Category: Finnis, C]]
-[[Category: Iyer, S.]]
+[[Category: Iyer, S]]
-[[Category: Mitsiki, E.]]
+[[Category: Mitsiki, E]]
-[[Category: Papageorgiou, A C.]]
+[[Category: Papageorgiou, A C]]
-[[Category: Prior, S H.]]
+[[Category: Prior, S H]]
-[[Category: Sleep, D.]]
+[[Category: Sleep, D]]
-[[Category: Thiyagarajan, N.]]
+[[Category: Thiyagarajan, N]]
 [[Category: 5-iodouracil]]
 [[Category: Angiogenesis]]
@@ Line 54: / Line 54: @@
 [[Category: Growth factor]]
 [[Category: Mutagenesis]]
-[[Category: Thymidine phosphorylase]]
 [[Category: Transferase]]

2wk6

From Proteopedia

Revision as of 07:52, 20 January 2015

STRUCTURAL FEATURES OF NATIVE HUMAN THYMIDINE PHOSPHORYLASE AND IN COMPLEX WITH 5-IODOURACIL

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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