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| | ==Crystal Structure Analysis of Human RNase T2== | | ==Crystal Structure Analysis of Human RNase T2== |
| - | <StructureSection load='3t0o' size='340' side='right' caption='[[3t0o]], [[Resolution|resolution]] 1.59Å' scene=''> | + | <StructureSection load='3t0o' size='340' side='right'caption='[[3t0o]], [[Resolution|resolution]] 1.59Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3t0o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T0O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3t0o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T0O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RNASET2, RNASE6PL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RNASET2, RNASE6PL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_T(2) Ribonuclease T(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.1 3.1.27.1] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribonuclease_T(2) Ribonuclease T(2)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.1 3.1.27.1] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3t0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0o OCA], [http://pdbe.org/3t0o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t0o RCSB], [http://www.ebi.ac.uk/pdbsum/3t0o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t0o ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3t0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t0o OCA], [https://pdbe.org/3t0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t0o RCSB], [https://www.ebi.ac.uk/pdbsum/3t0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t0o ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/RNT2_HUMAN RNT2_HUMAN]] Cystic leukoencephalopathy without megalencephaly. The disease is caused by mutations affecting the gene represented in this entry. | + | [[https://www.uniprot.org/uniprot/RNT2_HUMAN RNT2_HUMAN]] Cystic leukoencephalopathy without megalencephaly. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RNT2_HUMAN RNT2_HUMAN]] Has ribonuclease activity, with higher activity at acidic pH. Probably is involved in lysosomal degradation of ribosomal RNA (By similarity). Probably plays a role in cellular RNA catabolism.<ref>PMID:16620762</ref> <ref>PMID:19525954</ref> <ref>PMID:22735700</ref> | + | [[https://www.uniprot.org/uniprot/RNT2_HUMAN RNT2_HUMAN]] Has ribonuclease activity, with higher activity at acidic pH. Probably is involved in lysosomal degradation of ribosomal RNA (By similarity). Probably plays a role in cellular RNA catabolism.<ref>PMID:16620762</ref> <ref>PMID:19525954</ref> <ref>PMID:22735700</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Ribonuclease|Ribonuclease]] | + | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] |
| - | *[[Temp|Temp]]
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Human]] | | [[Category: Human]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Kraetzner, R]] | | [[Category: Kraetzner, R]] |
| | [[Category: Sheldrick, G]] | | [[Category: Sheldrick, G]] |
| Structural highlights
Disease
[RNT2_HUMAN] Cystic leukoencephalopathy without megalencephaly. The disease is caused by mutations affecting the gene represented in this entry.
Function
[RNT2_HUMAN] Has ribonuclease activity, with higher activity at acidic pH. Probably is involved in lysosomal degradation of ribosomal RNA (By similarity). Probably plays a role in cellular RNA catabolism.[1] [2] [3]
Publication Abstract from PubMed
Mutations in the gene of human RNase T2 are associated with white matter disease of the human brain. Although brain abnormalities (bilateral temporal lobe cysts and multifocal white matter lesions) and clinical symptoms (psychomotor impairments, spasticity and epilepsy) are well characterized, the pathomechanism of RNase T2 deficiency remains unclear. RNase T2 is the only member of the Rh/T2/S family of acidic hydrolases in humans. In recent years, new functions such as tumor suppressing properties of RNase T2 have been reported that are independent of its catalytic activity. We determined the X-ray structure of human RNase T2 at 1.6 A resolution. The alpha+beta core fold shows high similarity to those of known T2 RNase structures from plants, while, in contrast, the external loop regions show distinct structural differences. The catalytic features of RNase T2 in presence of bivalent cations were analyzed and the structural consequences of known clinical mutations were investigated. Our data provide further insight into the function of human RNase T2 and may prove useful in understanding its mode of action independent of its enzymatic activity.
Structure and activity of the only human RNase T2.,Thorn A, Steinfeld R, Ziegenbein M, Grapp M, Hsiao HH, Urlaub H, Sheldrick GM, Gartner J, Kratzner R Nucleic Acids Res. 2012 Jun 26. PMID:22735700[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Campomenosi P, Salis S, Lindqvist C, Mariani D, Nordstrom T, Acquati F, Taramelli R. Characterization of RNASET2, the first human member of the Rh/T2/S family of glycoproteins. Arch Biochem Biophys. 2006 May 15;449(1-2):17-26. Epub 2006 Mar 13. PMID:16620762 doi:http://dx.doi.org/10.1016/j.abb.2006.02.022
- ↑ Henneke M, Diekmann S, Ohlenbusch A, Kaiser J, Engelbrecht V, Kohlschutter A, Kratzner R, Madruga-Garrido M, Mayer M, Opitz L, Rodriguez D, Ruschendorf F, Schumacher J, Thiele H, Thoms S, Steinfeld R, Nurnberg P, Gartner J. RNASET2-deficient cystic leukoencephalopathy resembles congenital cytomegalovirus brain infection. Nat Genet. 2009 Jul;41(7):773-5. doi: 10.1038/ng.398. Epub 2009 Jun 14. PMID:19525954 doi:http://dx.doi.org/10.1038/ng.398
- ↑ Thorn A, Steinfeld R, Ziegenbein M, Grapp M, Hsiao HH, Urlaub H, Sheldrick GM, Gartner J, Kratzner R. Structure and activity of the only human RNase T2. Nucleic Acids Res. 2012 Jun 26. PMID:22735700 doi:10.1093/nar/gks614
- ↑ Thorn A, Steinfeld R, Ziegenbein M, Grapp M, Hsiao HH, Urlaub H, Sheldrick GM, Gartner J, Kratzner R. Structure and activity of the only human RNase T2. Nucleic Acids Res. 2012 Jun 26. PMID:22735700 doi:10.1093/nar/gks614
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