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TitleICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4
Journal, issue, pagesJ. Biol. Chem., Vol. 280, Page 31276-31282, Year 2005
Publish dateJun 10, 2005 (structure data deposition date)
AuthorsSchedlbauer, A. / Gandini, R. / Garavaglia, M.L. / Saino, S. / Gschwentner, M. / Sarg, B. / Lindner, H. / Jakab, M. / Ritter, M. / Bazzini, C. ...Schedlbauer, A. / Gandini, R. / Garavaglia, M.L. / Saino, S. / Gschwentner, M. / Sarg, B. / Lindner, H. / Jakab, M. / Ritter, M. / Bazzini, C. / Botta, G. / Meyer, G. / Kontaxis, G. / Tilly, B.C. / Konrat, R. / Paulmichl, M.
External linksJ. Biol. Chem. / PubMed:15905169
MethodsNMR (solution)
Structure data

PDB-1zyi:
Solution structure of ICLN, a multifunctional protein involved in regulatory mechanisms as different as cell volume regulation and rna splicing
Method: SOLUTION NMR

Source
  • canis lupus familiaris (dog)
KeywordsTRANSLATION / PH DOMAIN; ICLN; CELL VOLUME REGULATION; RNA SPLICING

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