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| - | [[Image:1bx4.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1bx4| PDB=1bx4 | SCENE= }} | | {{STRUCTURE_1bx4| PDB=1bx4 | SCENE= }} |
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| - | '''STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.50 ANGSTROMS'''
| + | ===STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.50 ANGSTROMS=== |
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| - | ==Overview==
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| - | Adenosine kinase (AK) is a key enzyme in the regulation of extracellular adenosine and intracellular adenylate levels. Inhibitors of adenosine kinase elevate adenosine to levels that activate nearby adenosine receptors and produce a wide variety of therapeutically beneficial activities. Accordingly, AK is a promising target for new analgesic, neuroprotective, and cardioprotective agents. We determined the structure of human adenosine kinase by X-ray crystallography using MAD phasing techniques and refined the structure to 1.5 A resolution. The enzyme structure consisted of one large alpha/beta domain with nine beta-strands, eight alpha-helices, and one small alpha/beta-domain with five beta-strands and two alpha-helices. The active site is formed along the edge of the beta-sheet in the large domain while the small domain acts as a lid to cover the upper face of the active site. The overall structure is similar to the recently reported structure of ribokinase from Escherichia coli [Sigrell et al. (1998) Structure 6, 183-193]. The structure of ribokinase was determined at 1.8 A resolution and represents the first structure of a new family of carbohydrate kinases. Two molecules of adenosine were present in the AK crystal structure with one adenosine molecule located in a site that matches the ribose site in ribokinase and probably represents the substrate-binding site. The second adenosine site overlaps the ADP site in ribokinase and probably represents the ATP site. A Mg2+ ion binding site is observed in a trough between the two adenosine sites. The structure of the active site is consistent with the observed substrate specificity. The active-site model suggests that Asp300 is an important catalytic residue involved in the deprotonation of the 5'-hydroxyl during the phosphate transfer.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9843365}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9843365 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9843365}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Mathews, I I.]] | | [[Category: Mathews, I I.]] |
| | [[Category: Human adenosine kinase]] | | [[Category: Human adenosine kinase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:03:56 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:51:35 2008'' |
Revision as of 16:51, 30 June 2008
Template:STRUCTURE 1bx4
STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.50 ANGSTROMS
Template:ABSTRACT PUBMED 9843365
About this Structure
1BX4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of human adenosine kinase at 1.5 A resolution., Mathews II, Erion MD, Ealick SE, Biochemistry. 1998 Nov 10;37(45):15607-20. PMID:9843365
Page seeded by OCA on Mon Jun 30 19:51:35 2008
