1hiy

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[[Image:1hiy.gif|left|200px]]
[[Image:1hiy.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1hiy |SIZE=350|CAPTION= <scene name='initialview01'>1hiy</scene>, resolution 2.6&Aring;
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The line below this paragraph, containing "STRUCTURE_1hiy", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:3an+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:3an+Binding+Site+For+Chain+B'>AC2</scene> and <scene name='pdbsite=AC3:3an+Binding+Site+For+Chain+C'>AC3</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=3AN:3&#39;-DEOXY+3&#39;-AMINO+ADENOSINE-5&#39;-DIPHOSPHATE'>3AN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1hiy| PDB=1hiy | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hiy OCA], [http://www.ebi.ac.uk/pdbsum/1hiy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hiy RCSB]</span>
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}}
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'''BINDING OF NUCLEOTIDES TO NDP KINASE'''
'''BINDING OF NUCLEOTIDES TO NDP KINASE'''
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[[Category: Morr, M.]]
[[Category: Morr, M.]]
[[Category: Xu, Y.]]
[[Category: Xu, Y.]]
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[[Category: kinase]]
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[[Category: Kinase]]
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[[Category: metabolic role]]
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[[Category: Metabolic role]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:53:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:05:46 2008''
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Revision as of 15:53, 2 May 2008

Template:STRUCTURE 1hiy

BINDING OF NUCLEOTIDES TO NDP KINASE


Overview

The source of affinity for substrates of human nucleoside diphosphate (NDP) kinases is particularly important in that its knowledge could be used to design more effective antiviral nucleoside drugs (e.g., AZT). We carried out a microcalorimetric study of the binding of enzymes from two organisms to various nucleotides. Isothermal titration calorimetry has been used to characterize the binding in terms of Delta G degrees, Delta H degrees and Delta S degrees. Thermodynamic parameters of the interaction of ADP with the hexameric NDP kinase from Dictyostelium discoideum and with the tetrameric enzyme from Myxococcus xanthus, at 20 degrees C, were similar and, in both cases, binding was enthalpy-driven. The interactions of ADP, 2'deoxyADP, GDP, and IDP with the eukaryotic enzyme differed in enthalpic and entropic terms, whereas the Delta G degrees values obtained were similar due to enthalpy--entropy compensation. The binding of the enzyme to nonphysiological nucleotides, such as AMP--PNP, 3'deoxyADP, and 3'-deoxy-3'-amino-ADP, appears to differ in several respects. Crystallography of the protein bound to 3'-deoxy-3'-amino-ADP showed that the drug was in a distorted position, and was unable to interact correctly with active site side chains. The interaction of pyrimidine nucleoside diphosphates with the hexameric enzyme is characterized by a lower affinity than that with purine nucleotides. Titration showed the stoichiometry of the interaction to be abnormal, with 9--12 binding sites/hexamer. The presence of supplementary binding sites might have physiological implications.

About this Structure

1HIY is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.

Reference

Binding of nucleotides to nucleoside diphosphate kinase: a calorimetric study., Cervoni L, Lascu I, Xu Y, Gonin P, Morr M, Merouani M, Janin J, Giartosio A, Biochemistry. 2001 Apr 17;40(15):4583-9. PMID:11294625 Page seeded by OCA on Fri May 2 18:53:22 2008

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