2ioc
From Proteopedia
(New page: 200px<br /><applet load="2ioc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ioc, resolution 2.100Å" /> '''The crystal structu...) |
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| - | [[Image:2ioc.jpg|left|200px]]<br /><applet load="2ioc" size=" | + | [[Image:2ioc.jpg|left|200px]]<br /><applet load="2ioc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ioc, resolution 2.100Å" /> | caption="2ioc, resolution 2.100Å" /> | ||
'''The crystal structure of TREX1 explains the 3' nucleotide specificity and reveals a polyproline II helix for protein partenring'''<br /> | '''The crystal structure of TREX1 explains the 3' nucleotide specificity and reveals a polyproline II helix for protein partenring'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2IOC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MN and D5M as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Exodeoxyribonuclease_III Exodeoxyribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.2 3.1.11.2] Full crystallographic information is available from [http:// | + | 2IOC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=D5M:'>D5M</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Exodeoxyribonuclease_III Exodeoxyribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.2 3.1.11.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IOC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: proline helix]] | [[Category: proline helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:30:54 2008'' |
Revision as of 13:30, 23 January 2008
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The crystal structure of TREX1 explains the 3' nucleotide specificity and reveals a polyproline II helix for protein partenring
Overview
The TREX1 enzyme processes DNA ends as the major 3' --> 5' exonuclease, activity in human cells. Mutations in the TREX1 gene are an underlying, cause of the neurological brain disease Aicardi-Goutieres syndrome, implicating TREX1 dysfunction in an aberrant immune response. TREX1 action, during apoptosis likely prevents autoimmune reaction to DNA that would, otherwise persist. To understand the impact of TREX1 mutations identified, in patients with Aicardi-Goutieres syndrome on structure and activity we, determined the x-ray crystal structure of the dimeric mouse TREX1 protein, in substrate and product complexes containing single-stranded DNA and, deoxyadenosine monophosphate, respectively. The structures show the, specific interactions between the bound nucleotides and the residues, lining the binding pocket of the 3' terminal nucleotide within the enzyme, active site that account for specificity, and provide the molecular basis, for understanding mutations that lead to disease. Three mutant forms of, TREX1 protein identified in patients with Aicardi-Goutieres syndrome were, prepared and the measured activities show that these specific mutations, reduce enzyme activity by 4-35,000-fold. The structure also reveals an, 8-amino acid polyproline II helix within the TREX1 enzyme that suggests a, mechanism for interactions of this exonuclease with other protein, complexes.
About this Structure
2IOC is a Single protein structure of sequence from Mus musculus with and as ligands. Active as Exodeoxyribonuclease III, with EC number 3.1.11.2 Full crystallographic information is available from OCA.
Reference
The Crystal Structure of TREX1 Explains the 3' Nucleotide Specificity and Reveals a Polyproline II Helix for Protein Partnering., de Silva U, Choudhury S, Bailey SL, Harvey S, Perrino FW, Hollis T, J Biol Chem. 2007 Apr 6;282(14):10537-43. Epub 2007 Feb 9. PMID:17293595
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