2fju

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[[Image:2fju.gif|left|200px]]<br /><applet load="2fju" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2fju.gif|left|200px]]
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caption="2fju, resolution 2.20&Aring;" />
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'''Activated Rac1 bound to its effector phospholipase C beta 2'''<br />
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{{Structure
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|PDB= 2fju |SIZE=350|CAPTION= <scene name='initialview01'>2fju</scene>, resolution 2.20&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=GSP:5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoinositide_phospholipase_C Phosphoinositide phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.11 3.1.4.11]
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|GENE= RAC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), PLCB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Activated Rac1 bound to its effector phospholipase C beta 2'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2FJU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=GSP:'>GSP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoinositide_phospholipase_C Phosphoinositide phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.11 3.1.4.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FJU OCA].
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2FJU is a [[Protein complex]] structure of sequences 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=2FJU OCA].
==Reference==
==Reference==
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Crystal structure of Rac1 bound to its effector phospholipase C-beta2., Jezyk MR, Snyder JT, Gershberg S, Worthylake DK, Harden TK, Sondek J, Nat Struct Mol Biol. 2006 Dec;13(12):1135-40. Epub 2006 Nov 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17115053 17115053]
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Crystal structure of Rac1 bound to its effector phospholipase C-beta2., Jezyk MR, Snyder JT, Gershberg S, Worthylake DK, Harden TK, Sondek J, Nat Struct Mol Biol. 2006 Dec;13(12):1135-40. Epub 2006 Nov 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17115053 17115053]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Phosphoinositide phospholipase C]]
[[Category: Phosphoinositide phospholipase C]]
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[[Category: protein-protein complex]]
[[Category: protein-protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:22:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:53:14 2008''

Revision as of 14:53, 20 March 2008

Image:2fju.gif


PDB ID 2fju

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands: , and
Gene: RAC1 (Homo sapiens), PLCB2 (Homo sapiens)
Activity: Phosphoinositide phospholipase C, with EC number 3.1.4.11
Coordinates: save as pdb, mmCIF, xml



Activated Rac1 bound to its effector phospholipase C beta 2


Contents

Overview

Although diverse signaling cascades require the coordinated regulation of heterotrimeric G proteins and small GTPases, these connections remain poorly understood. We present the crystal structure of the GTPase Rac1 bound to phospholipase C-beta2 (PLC-beta2), a classic effector of heterotrimeric G proteins. Rac1 engages the pleckstrin-homology (PH) domain of PLC-beta2 to optimize its orientation for substrate membranes. Gbetagamma also engages the PH domain to activate PLC-beta2, and these two activation events are compatible, leading to additive stimulation of phospholipase activity. In contrast to PLC-delta, the PH domain of PLC-beta2 cannot bind phosphoinositides, eliminating this mode of regulation. The structure of the Rac1-PLC-beta2 complex reveals determinants that dictate selectivity of PLC-beta isozymes for Rac GTPases over other Rho-family GTPases, and substitutions within PLC-beta2 abrogate its stimulation by Rac1 but not by Gbetagamma, allowing for functional dissection of this integral signaling node.

Disease

Known disease associated with this structure: Platelet PLC beta-2 deficiency OMIM:[604114]

About this Structure

2FJU is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of Rac1 bound to its effector phospholipase C-beta2., Jezyk MR, Snyder JT, Gershberg S, Worthylake DK, Harden TK, Sondek J, Nat Struct Mol Biol. 2006 Dec;13(12):1135-40. Epub 2006 Nov 19. PMID:17115053

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