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Crystal Structure Analysis of Human RNase T2
Structural highlights
DiseaseRNT2_HUMAN Cystic leukoencephalopathy without megalencephaly. The disease is caused by mutations affecting the gene represented in this entry. FunctionRNT2_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 PubMedMutations 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 AlsoReferences
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