Adenosine deaminase
From Proteopedia
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== Function == | == Function == | ||
| - | '''Adenosine deaminase''' (ADA) deaminates adenosine and deoxyadenosine into inosine or deoxyinosine. ADA is part of the purine metabolism. In humans ADA is involved in the development and maintenance of the immune system. ADA binds dipeptidyl peptidase IV. The complex acts as a positive regulator of T-cell coactivation and regulates lymphocytes-epithelial adhesion.<ref>PMID:1925539</ref> | + | '''Adenosine deaminase''' (ADA) or '''double-stranded RNA-specific editase''' deaminates adenosine and deoxyadenosine into inosine or deoxyinosine. ADA is part of the purine metabolism. In humans ADA is involved in the development and maintenance of the immune system. ADA binds dipeptidyl peptidase IV. The complex acts as a positive regulator of T-cell coactivation and regulates lymphocytes-epithelial adhesion.<ref>PMID:1925539</ref> |
| + | *'''Double-stranded RNA-specific adenosine deaminase''' catalyses the C-6 deamination of adenosine in viral RNAs and cellular pre-mRNA<ref>PMID:9735305</ref>. | ||
| + | *'''tRNA-specific adenosine deaminase''' catalyses the deamination of adenosine to inosine in tRNA<ref>PMID:10430867</ref>. | ||
== Disease == | == Disease == | ||
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</StructureSection> | </StructureSection> | ||
| - | == 3D Structures of adenosine deaminase == | ||
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| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| - | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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| - | *Adenosine deaminase | ||
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| - | **[[1vfl]] – bADA + Zn - bovine<BR /> | ||
| - | **[[3iar]] – hADA + Ni - human<BR /> | ||
| - | **[[3lgd]] – hADA2 + Zn<BR /> | ||
| - | **[[3mvt]] – mADA – mouse<BR /> | ||
| - | **[[3mvi]] – mADA + Zn<BR /> | ||
| - | **[[3ou8]] – PaADA + Zn – ''Pseudomonas aeruginosa''<BR /> | ||
| - | **[[2amx]] – ADA + Co – ''Plasmodium yoeli''<BR /> | ||
| - | **[[4gxw]] – ADA + Zn – ''Burkholderia ambifaria'' <BR /> | ||
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| - | *Adenosine deaminase complex with nucleotide | ||
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| - | **[[1add]] – mADA + Zn + deaza-adenosine <BR /> | ||
| - | **[[3km8]] – mADA (mutant) + Zn + deaza-adenosine <BR /> | ||
| - | **[[2ada]] – mADA + Zn + transition state analog<BR /> | ||
| - | **[[1fkw]], [[1fkx]], [[1uio]], [[1uip]] – mADA (mutant) + Zn + adenosine analog<BR /> | ||
| - | **[[1a4m]] – mADA + Zn + adenosine analog<BR /> | ||
| - | **[[1krm]] – bADA + Zn + adenosine analog <BR /> | ||
| - | **[[2pgf]] – PvADA + Zn + adenosine – ''Plasmodium vivax''<BR /> | ||
| - | **[[2pgr]] – PvADA + Zn + adenosine analog<BR /> | ||
| - | **[[2qvn]] – PvADA + guanosine <BR /> | ||
| - | **[[3pan]] – PaADA + Zn + hypoxanthine <BR /> | ||
| - | **[[3pao]] – PaADA + Zn + adenine <BR /> | ||
| - | **[[3rys]] – ADA + Zn + adenine – ''Arthrobacter aurescens''<BR /> | ||
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| - | *Adenosine deaminase complex with inhibitor | ||
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| - | **[[1a4l]] – mADA + Zn + inhibitor<BR /> | ||
| - | **[[1ndv]], [[1ndw]], [[1ndy]], [[1ndz]], [[1o5r]], [[1qxl]], [[1uml]], [[1v79]], [[1v7a]], [[1wxy]], [[1wxz]], [[2e1w]], [[2z7g]] – bADA + Zn + inhibitor<BR /> | ||
| - | **[[3ewc]] – PvADA + Zn + inhibitor<BR /> | ||
| - | **[[3ewd]] – PvADA (mutant) + Zn + inhibitor<BR /> | ||
| - | **[[3pbm]] – PaADA + Zn + chloropurine <BR /> | ||
| - | **[[3lgg]] – hADA2 + Zn + coformycin<BR /> | ||
| - | **[[6n9m]] – ADA + Zn + pentostatin – ''Salmonella typhimurium''<BR /> | ||
| - | **[[6n91]] – ADA + Zn + pentostatin – ''Vibrio cholerae''<BR /> | ||
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| - | *Adenosine deaminase complex with protein | ||
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| - | **[[1w1i]] – bADA + Zn + dipeptidyl peptidase IV<BR /> | ||
| - | **[[2bgn]] – bADA + Zn + dipeptidyl peptidase IV + HIV1 TAT protein peptide<BR /> | ||
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| - | *Double-stranded RNA-specific adenosine deaminase; domains – Zα 125-201; Zβ 294-366; 3rd RNA-binding 708-801; catalytic 299-729 | ||
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| - | **[[1xmk]] – hADA Zα domain <br /> | ||
| - | **[[1qgp]] – hADA Zα domain - NMR<br /> | ||
| - | **[[2l54]] – hADA Zα domain (mutant) - NMR<br /> | ||
| - | **[[2acj]], [[1qbj]], [[2gxb]], [[3f21]], [[3f22]], [[3f23]], [[3irq]], [[3irr]], [[5zu1]], [[5zuo]], [[5zup]] – hADA Zα domain + DNA<br /> | ||
| - | **[[2mdr]] – hADA 3rd RNA-binding domain - NMR<br /> | ||
| - | **[[1zy7]] – hADA catalytic domain + inositol hexakisphosphate<br /> | ||
| - | **[[6d06]], [[5hp2]], [[5hp3]], [[5ed1]], [[5ed2]] – hADA catalytic domain + RNA<br /> | ||
| - | **[[2b7t]], [[2b7v]] – rADA 1st RNA-binding domain – rat<br /> | ||
| - | **[[2l3c]], [[2l3j]] – rADA 1st RNA-binding domain + RNA – NMR<br /> | ||
| - | **[[2l2k]] – mADA residues 230-301 + RNA – NMR<br /> | ||
| - | **[[2ljh]] – ADA DRBM domain – ''Drosophila melanogaster'' – NMR<br /> | ||
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| - | *tRNA-specific adenosine deaminase | ||
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| - | **[[1z3a]] – ADA – Escherichia coli<br /> | ||
| - | **[[2b3j]] – ADA + Zn + tRNA stem-loop – ''Stapphylococcus aureus''<BR /> | ||
| - | **[[1wwr]] – ADA – ''Aquifex aeolicus''<br /> | ||
| - | **[[2nx8]] – ADA (mutant) + Zn – ''Streptococcus pyogenes''<br /> | ||
| - | **[[3dh1]] – hADA subunit ADAT2<br /> | ||
| - | }} | ||
==References == | ==References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ Wilson DK, Rudolph FB, Quiocho FA. Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations. Science. 1991 May 31;252(5010):1278-84. PMID:1925539
- ↑ Liu Y, Herbert A, Rich A, Samuel CE. Double-stranded RNA-specific adenosine deaminase: nucleic acid binding properties. Methods. 1998 Jul;15(3):199-205. PMID:9735305 doi:10.1006/meth.1998.0624
- ↑ Maas S, Gerber AP, Rich A. Identification and characterization of a human tRNA-specific adenosine deaminase related to the ADAR family of pre-mRNA editing enzymes. Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8895-900. PMID:10430867 doi:10.1073/pnas.96.16.8895
- ↑ Larson ET, Deng W, Krumm BE, Napuli A, Mueller N, Van Voorhis WC, Buckner FS, Fan E, Lauricella A, DeTitta G, Luft J, Zucker F, Hol WG, Verlinde CL, Merritt EA. Structures of substrate- and inhibitor-bound adenosine deaminase from a human malaria parasite show a dramatic conformational change and shed light on drug selectivity. J Mol Biol. 2008 Sep 12;381(4):975-88. Epub 2008 Jun 24. PMID:18602399 doi:http://dx.doi.org/10.1016/j.jmb.2008.06.048
