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1ypv

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[[Image:1ypv.gif|left|200px]]<br /><applet load="1ypv" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ypv.gif|left|200px]]
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caption="1ypv, resolution 1.80&Aring;" />
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'''Structure of human thymidylate synthase at low salt conditions'''<br />
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{{Structure
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|PDB= 1ypv |SIZE=350|CAPTION= <scene name='initialview01'>1ypv</scene>, resolution 1.80&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Thymidylate_synthase Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45]
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|GENE= TYMS, TS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Structure of human thymidylate synthase at low salt conditions'''
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==Overview==
==Overview==
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==Disease==
==Disease==
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Known disease associated with this structure: Timothy syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=114205 114205]]
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Known diseases associated with this structure: Brugada syndrome 3 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=114205 114205]], Timothy syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=114205 114205]]
==About this Structure==
==About this Structure==
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1YPV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Thymidylate_synthase Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YPV OCA].
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1YPV is a [[Single protein]] structure of 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=1YPV OCA].
==Reference==
==Reference==
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Structure of human thymidylate synthase under low-salt conditions., Lovelace LL, Minor W, Lebioda L, Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):622-7. Epub 2005, Apr 20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15858273 15858273]
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Structure of human thymidylate synthase under low-salt conditions., Lovelace LL, Minor W, Lebioda L, Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):622-7. Epub 2005, Apr 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15858273 15858273]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: thymidylate synthase]]
[[Category: thymidylate synthase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:25:57 2008''

Revision as of 13:25, 20 March 2008


PDB ID 1ypv

Drag the structure with the mouse to rotate
, resolution 1.80Å
Ligands:
Gene: TYMS, TS (Homo sapiens)
Activity: Thymidylate synthase, with EC number 2.1.1.45
Coordinates: save as pdb, mmCIF, xml



Structure of human thymidylate synthase at low salt conditions


Contents

Overview

Human thymidylate synthase, a target in cancer chemotherapy, was crystallized from PEG 3350 with 30 mM ammonium sulfate (AS) in the crystallization medium. The crystals are isomorphous with the high-salt crystals ( approximately 2.0 M AS) and the structure has been solved and refined (R = 22.6%, R(free) = 24.3%) at 1.8 A resolution. The high- and low-AS-concentration structures are quite similar, with loop 181-197 is in the inactive conformation. Also, residues 95-106 and 129-135 (eukaryotic inserts region) show high mobility as assessed by poor electron density and high values of crystallographic temperature factors (residues 1-25 and 108-129 are disordered in both structures). The high mobility of this region may reflect the situation at physiological ionic strength. Of the four sulfate ions observed bound at 2.0 M AS, only two are present at 30 mM AS. The inactive conformation appears to be stabilized by the side chain of Val3 or a leucine residue from the disordered regions. The low-salt conditions of these crystals should be much more suitable for the study of thymidylate synthase inhibitors, especially those that utilize sulfate-binding sites to stabilize the inactive conformation of loop 181-197.

Disease

Known diseases associated with this structure: Brugada syndrome 3 OMIM:[114205], Timothy syndrome OMIM:[114205]

About this Structure

1YPV is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of human thymidylate synthase under low-salt conditions., Lovelace LL, Minor W, Lebioda L, Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):622-7. Epub 2005, Apr 20. PMID:15858273

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