1ucn

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[[Image:1ucn.jpg|left|200px]]<br /><applet load="1ucn" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ucn.jpg|left|200px]]
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caption="1ucn, resolution 2.0&Aring;" />
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'''X-ray structure of human nucleoside diphosphate kinase A complexed with ADP at 2 A resolution'''<br />
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{{Structure
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|PDB= 1ucn |SIZE=350|CAPTION= <scene name='initialview01'>1ucn</scene>, resolution 2.0&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''X-ray structure of human nucleoside diphosphate kinase A complexed with ADP at 2 A resolution'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1UCN 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>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UCN OCA].
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1UCN 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=1UCN OCA].
==Reference==
==Reference==
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Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases., Chen Y, Gallois-Montbrun S, Schneider B, Veron M, Morera S, Deville-Bonne D, Janin J, J Mol Biol. 2003 Sep 26;332(4):915-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12972261 12972261]
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Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases., Chen Y, Gallois-Montbrun S, Schneider B, Veron M, Morera S, Deville-Bonne D, Janin J, J Mol Biol. 2003 Sep 26;332(4):915-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12972261 12972261]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Nucleoside-diphosphate kinase]]
[[Category: Nucleoside-diphosphate kinase]]
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[[Category: mutant complexe adp]]
[[Category: mutant complexe adp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:23:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:30:14 2008''

Revision as of 12:30, 20 March 2008


PDB ID 1ucn

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands: , , and
Activity: Nucleoside-diphosphate kinase, with EC number 2.7.4.6
Coordinates: save as pdb, mmCIF, xml



X-ray structure of human nucleoside diphosphate kinase A complexed with ADP at 2 A resolution


Contents

Overview

NDPK-A, product of the nm23-H1 gene, is one of the two major isoforms of human nucleoside diphosphate kinase. We analyzed the binding of its nucleotide substrates by fluorometric methods. The binding of nucleoside triphosphate (NTP) substrates was detected by following changes of the intrinsic fluorescence of the H118G/F60W variant, a mutant protein engineered for that purpose. Nucleoside diphosphate (NDP) substrate binding was measured by competition with a fluorescent derivative of ADP, following the fluorescence anisotropy of the derivative. We also determined an X-ray structure at 2.0A resolution of the variant NDPK-A in complex with ADP, Ca(2+) and inorganic phosphate, products of ATP hydrolysis. We compared the conformation of the bound nucleotide seen in this complex and the interactions it makes with the protein, with those of the nucleotide substrates, substrate analogues or inhibitors present in other NDP kinase structures. We also compared NDP kinase-bound nucleotides to ATP bound to protein kinases, and showed that the nucleoside monophosphate moieties have nearly identical conformations in spite of the very different protein environments. However, the beta and gamma-phosphate groups are differently positioned and oriented in the two types of kinases, and they bind metal ions with opposite chiralities. Thus, it should be possible to design nucleotide analogues that are good substrates of one type of kinase, and poor substrates or inhibitors of the other kind.

Disease

Known disease associated with this structure: Neuroblastoma OMIM:[156490]

About this Structure

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

Reference

Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases., Chen Y, Gallois-Montbrun S, Schneider B, Veron M, Morera S, Deville-Bonne D, Janin J, J Mol Biol. 2003 Sep 26;332(4):915-26. PMID:12972261

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