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2dok
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(New page: 200px<br /> <applet load="2dok" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dok, resolution 1.80Å" /> '''Crystal structure o...)
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Revision as of 19:32, 12 November 2007
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Crystal structure of the PIN domain of human EST1A
Overview
Saccharomyces cerevisiae Est1p is a telomerase-associated protein, essential for telomere length homeostasis. hEST1A is one of the three, human Est1p homologues and is considered to be involved not only in, regulation of telomere elongation or capping but also in nonsense-mediated, degradation of RNA. hEST1A is composed of two conserved regions, Est1p, homology and PIN (PilT N-terminus) domains. The present study shows the, crystal structure of the PIN domain at 1.8 A resolution. The overall, structure is composed of an alpha/beta fold or a core structure similar to, the counterpart of 5' nucleases and an extended structure absent from, archaeal PIN-domain proteins and 5' nucleases. The structural properties, of the PIN domain indicate its putative active center consisting of, invariant acidic amino acid residues, which is geometrically similar to, the active center of 5' nucleases and an archaeal PAE2754 PIN-domain, protein associated with exonuclease activity.
About this Structure
2DOK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the PIN domain of human telomerase-associated protein EST1A., Takeshita D, Zenno S, Lee WC, Saigo K, Tanokura M, Proteins. 2007 Sep 1;68(4):980-9. PMID:17557331
Page seeded by OCA on Mon Nov 12 21:38:53 2007
