2b92
Crystal-structure of the N-terminal Large GTPase Domain of human Guanylate Binding protein 1 (hGBP1) in complex with GDP/AlF3Crystal-structure of the N-terminal Large GTPase Domain of human Guanylate Binding protein 1 (hGBP1) in complex with GDP/AlF3
Template:ABSTRACT PUBMED 16511497
About this StructureAbout this Structure
2b92 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
[xtra 1][xtra 2][xtra 3][xtra 4][xtra 5]
- ↑ Ghosh A, Praefcke GJ, Renault L, Wittinghofer A, Herrmann C. How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP. Nature. 2006 Mar 2;440(7080):101-4. PMID:16511497 doi:10.1038/nature04510
- ↑ Prakash B, Renault L, Praefcke GJ, Herrmann C, Wittinghofer A. Triphosphate structure of guanylate-binding protein 1 and implications for nucleotide binding and GTPase mechanism. EMBO J. 2000 Sep 1;19(17):4555-64. PMID:10970849 doi:10.1093/emboj/19.17.4555
- ↑ Prakash B, Praefcke GJ, Renault L, Wittinghofer A, Herrmann C. Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. Nature. 2000 Feb 3;403(6769):567-71. PMID:10676968 doi:10.1038/35000617
- ↑ Gasper R, Meyer S, Gotthardt K, Sirajuddin M, Wittinghofer A. It takes two to tango: regulation of G proteins by dimerization. Nat Rev Mol Cell Biol. 2009 Jun;10(6):423-9. Epub 2009 May 8. PMID:19424291 doi:nrm2689
- ↑ Chappie JS, Acharya S, Leonard M, Schmid SL, Dyda F. G domain dimerization controls dynamin's assembly-stimulated GTPase activity. Nature. 2010 May 27;465(7297):435-40. Epub 2010 Apr 28. PMID:20428113 doi:10.1038/nature09032