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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 04911naa a2200913 4500 | |
| 001 | oai:DiVA.org:sh-22557 | |
| 003 | SwePub | |
| 008 | 140303s2007 | |||||||||||000 ||eng| | |
| 009 | oai:DiVA.org:su-19855 | |
| 009 | oai:prod.swepub.kib.ki.se:115889040 | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:sh:diva-225572 URI |
| 024 | 7 | a https://doi.org/10.1016/j.jmb.2007.06.0502 DOI |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-198552 URI |
| 024 | 7 | a http://kipublications.ki.se/Default.aspx?queryparsed=id:1158890402 URI |
| 040 | a (SwePub)shd (SwePub)sud (SwePub)ki | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Högbom, Martinu Stockholms universitet,Institutionen för biokemi och biofysik4 aut0 (Swepub:su)hogbom |
| 245 | 1 0 | a Crystal Structure of Conserved Domains 1 and 2 of the Human DEAD-box Helicase DDX3X in Complex with the Mononucleotide AMP |
| 264 | 1 | b Elsevier BV,c 2007 |
| 338 | a print2 rdacarrier | |
| 520 | a DExD-box helicases are involved in all aspects of cellular RNA metabolism. Conserved domains 1 and 2 contain nine signature motifs that are responsible for nucleotide binding, RNA binding and ATP hydrolysis. The human DEAD-box helicase DDX3X has been associated with several different cellular processes, such as cell-growth control, mRNA transport and translation, and is suggested to be essential for the export of unspliced/partially spliced HIV mRNAs from the nucleus to the cytoplasm. Here, the crystal structure of conserved domains 1 and 2 of DDX3X, including a DDX3-specific insertion that is not generally found in human DExD-box helicases, is presented. The N-terminal domain 1 and the C-terminal domain 2 both display RecA-like folds comprising a central β-sheet flanked by α-helices. Interestingly, the DDX3X-specific insertion forms a helical element that extends a highly positively charged sequence in a loop, thus increasing the RNA-binding surface of the protein. Surprisingly, although DDX3X was crystallized in the presence of a large excess of ADP or the slowly hydrolyzable ATP analogue ATPγS the contaminant AMP was seen in the structure. A fluorescent-based stability assay showed that the thermal stability of DDX3X was increased by the mononucleotide AMP but not by ADP or ATPγS, suggesting that DDX3X is stabilized by AMP and elucidating why AMP was found in the nucleotide-binding pocket. | |
| 650 | 7 | a NATURVETENSKAPx Biologi0 (SwePub)1062 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Biological Sciences0 (SwePub)1062 hsv//eng |
| 653 | a DEAD-box | |
| 653 | a helicase | |
| 653 | a HIV | |
| 653 | a nucleotide | |
| 653 | a RNA | |
| 653 | a adenosine diphosphate | |
| 653 | a adenosine phosphate | |
| 653 | a adenosine triphosphate | |
| 653 | a DEAD box protein | |
| 653 | a dead box protein ddx3x | |
| 653 | a mononucleotide amp | |
| 653 | a RNA binding protein | |
| 653 | a unclassified drug | |
| 653 | a amino acid sequence | |
| 653 | a amino terminal sequence | |
| 653 | a article | |
| 653 | a carboxy terminal sequence | |
| 653 | a crystal structure | |
| 653 | a crystallization | |
| 653 | a priority journal | |
| 653 | a Adenosine Monophosphate | |
| 653 | a Binding Sites | |
| 653 | a Conserved Sequence | |
| 653 | a Crystallography | |
| 653 | a X-Ray | |
| 653 | a DEAD-box RNA Helicases | |
| 653 | a Enzyme Stability | |
| 653 | a Humans | |
| 653 | a Hydrolysis | |
| 653 | a Models | |
| 653 | a Molecular | |
| 653 | a Molecular Sequence Data | |
| 653 | a Protein Structure | |
| 653 | a Tertiary | |
| 653 | a RNA-Binding Proteins | |
| 653 | a Sequence Homology | |
| 653 | a Amino Acid | |
| 700 | 1 | a Collins, R.u Karolinska Institutet4 aut |
| 700 | 1 | a van den Berg, S.u Karolinska Institutet4 aut |
| 700 | 1 | a Jenvert, Rose-Marieu Södertörns högskola,Institutionen för livsvetenskaper4 aut0 (Swepub:sh)SH99REKN |
| 700 | 1 | a Karlberg, T.u Karolinska Institutet4 aut |
| 700 | 1 | a Kotenyova, T.4 aut |
| 700 | 1 | a Flores, A.4 aut |
| 700 | 1 | a Hedestam, G. B. K.u Karolinska Institutet4 aut |
| 700 | 1 | a Schiavone, L. H.4 aut |
| 710 | 2 | a Stockholms universitetb Institutionen för biokemi och biofysik4 org |
| 773 | 0 | t Journal of Molecular Biologyd : Elsevier BVg 372:1, s. 150-159q 372:1<150-159x 0022-2836x 1089-8638 |
| 856 | 4 | u https://zenodo.org/record/1066896/files/article.pdf |
| 856 | 4 | u http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=17631897&dopt=Citation |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:sh:diva-22557 |
| 856 | 4 8 | u https://doi.org/10.1016/j.jmb.2007.06.050 |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-19855 |
| 856 | 4 8 | u http://kipublications.ki.se/Default.aspx?queryparsed=id:115889040 |
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