2ocp
From Proteopedia
(New page: 200px<br /> <applet load="2ocp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ocp, resolution 2.80Å" /> '''Crystal Structure o...) |
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| - | [[Image:2ocp.gif|left|200px]]<br /> | + | [[Image:2ocp.gif|left|200px]]<br /><applet load="2ocp" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2ocp" size=" | + | |
caption="2ocp, resolution 2.80Å" /> | caption="2ocp, resolution 2.80Å" /> | ||
'''Crystal Structure of Human Deoxyguanosine Kinase'''<br /> | '''Crystal Structure of Human Deoxyguanosine Kinase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Deoxyribonucleoside kinases phosphorylate deoxyribonucleosides and | + | Deoxyribonucleoside kinases phosphorylate deoxyribonucleosides and activate a number of medically important nucleoside analogs. Here we report the structure of the Drosophila deoxyribonucleoside kinase with deoxycytidine bound at the nucleoside binding site and that of the human deoxyguanosine kinase with ATP at the nucleoside substrate binding site. Compared to the human kinase, the Drosophila kinase has a wider substrate cleft, which may be responsible for the broad substrate specificity of this enzyme. The human deoxyguanosine kinase is highly specific for purine substrates; this is apparently due to the presence of Arg 118, which provides favorable hydrogen bonding interactions with the substrate. The two new structures provide an explanation for the substrate specificity of cellular deoxyribonucleoside kinases. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2OCP 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 DTP as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 2OCP 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=DTP:'>DTP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1JAG. Active as [http://en.wikipedia.org/wiki/Deoxyguanosine_kinase Deoxyguanosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.113 2.7.1.113] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OCP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein-nucleotide complex]] | [[Category: protein-nucleotide complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:16:56 2008'' |
Revision as of 16:16, 21 February 2008
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Crystal Structure of Human Deoxyguanosine Kinase
Contents |
Overview
Deoxyribonucleoside kinases phosphorylate deoxyribonucleosides and activate a number of medically important nucleoside analogs. Here we report the structure of the Drosophila deoxyribonucleoside kinase with deoxycytidine bound at the nucleoside binding site and that of the human deoxyguanosine kinase with ATP at the nucleoside substrate binding site. Compared to the human kinase, the Drosophila kinase has a wider substrate cleft, which may be responsible for the broad substrate specificity of this enzyme. The human deoxyguanosine kinase is highly specific for purine substrates; this is apparently due to the presence of Arg 118, which provides favorable hydrogen bonding interactions with the substrate. The two new structures provide an explanation for the substrate specificity of cellular deoxyribonucleoside kinases.
Disease
Known diseases associated with this structure: Mitochondrial DNA-depletion syndrome, hepatocerebral form OMIM:[601465]
About this Structure
2OCP is a Single protein structure of sequence from Homo sapiens with as ligand. This structure supersedes the now removed PDB entry 1JAG. Active as Deoxyguanosine kinase, with EC number 2.7.1.113 Full crystallographic information is available from OCA.
Reference
Structural basis for substrate specificities of cellular deoxyribonucleoside kinases., Johansson K, Ramaswamy S, Ljungcrantz C, Knecht W, Piskur J, Munch-Petersen B, Eriksson S, Eklund H, Nat Struct Biol. 2001 Jul;8(7):616-20. PMID:11427893
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