2bc9: Difference between revisions

Revision as of 19:45, 16 February 2009

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File:2bc9.png

Template:STRUCTURE 2bc9

Crystal-structure of the N-terminal large GTPase Domain of human Guanylate Binding protein 1 (hGBP1) in complex with non-hydrolysable GTP analogue GppNHpCrystal-structure of the N-terminal large GTPase Domain of human Guanylate Binding protein 1 (hGBP1) in complex with non-hydrolysable GTP analogue GppNHp

Template:ABSTRACT PUBMED 16511497

About this StructureAbout this Structure

2BC9 is a 1 chain structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}^{[xtra 2]}^{[xtra 3]}

↑ 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

Page seeded by OCA on Mon Feb 16 18:45:34 2009

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OCA

[1] 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

[2] 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

[3] 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

[xtra 1]

[xtra 2]

[xtra 3]

@@ Line 20: / Line 20: @@
 ==About this Structure==
-BC9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BC9 OCA].
+BC9 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BC9 OCA].
 ==Reference==
-How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP., Ghosh A, Praefcke GJ, Renault L, Wittinghofer A, Herrmann C, Nature. 2006 Mar 2;440(7080):101-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16511497 16511497]
+<ref group="xtra">PMID:16511497</ref><ref group="xtra">PMID:10970849</ref><ref group="xtra">PMID:10676968</ref><references group="xtra"/>
-Triphosphate structure of guanylate-binding protein 1 and implications for nucleotide binding and GTPase mechanism., Prakash B, Renault L, Praefcke GJ, Herrmann C, Wittinghofer A, EMBO J. 2000 Sep 1;19(17):4555-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10970849 10970849]
-Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins., Prakash B, Praefcke GJ, Renault L, Wittinghofer A, Herrmann C, Nature. 2000 Feb 3;403(6769):567-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10676968 10676968]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
 [[Category: Ghosh, A.]]
 [[Category: Herrmann, C]]
@@ Line 37: / Line 32: @@
 [[Category: Protein- guanine nucleotide complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:02:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 18:45:34 2009''