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| | <StructureSection load='1ds6' size='340' side='right'caption='[[1ds6]], [[Resolution|resolution]] 2.35Å' scene=''> | | <StructureSection load='1ds6' size='340' side='right'caption='[[1ds6]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ds6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DS6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ds6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DS6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35Å</td></tr> |
| | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ds6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ds6 OCA], [https://pdbe.org/1ds6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ds6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ds6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ds6 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ds6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ds6 OCA], [https://pdbe.org/1ds6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ds6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ds6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ds6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[https://www.uniprot.org/uniprot/RAC2_HUMAN RAC2_HUMAN]] Defects in RAC2 are the cause of neutrophil immunodeficiency syndrome (NEUID) [MIM:[https://omim.org/entry/608203 608203]].<ref>PMID:10758162</ref>
| + | [https://www.uniprot.org/uniprot/RAC2_HUMAN RAC2_HUMAN] Defects in RAC2 are the cause of neutrophil immunodeficiency syndrome (NEUID) [MIM:[https://omim.org/entry/608203 608203].<ref>PMID:10758162</ref> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RAC2_HUMAN RAC2_HUMAN]] Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. Augments the production of reactive oxygen species (ROS) by NADPH oxidase.<ref>PMID:1660188</ref> [[https://www.uniprot.org/uniprot/GDIR2_HUMAN GDIR2_HUMAN]] Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them.
| + | [https://www.uniprot.org/uniprot/RAC2_HUMAN RAC2_HUMAN] Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. Augments the production of reactive oxygen species (ROS) by NADPH oxidase.<ref>PMID:1660188</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gierschik, P]] | + | [[Category: Gierschik P]] |
| - | [[Category: Illenberger, D]] | + | [[Category: Illenberger D]] |
| - | [[Category: Jensen, O N]] | + | [[Category: Jensen ON]] |
| - | [[Category: Scheffzek, K]] | + | [[Category: Scheffzek K]] |
| - | [[Category: Stephan, I]] | + | [[Category: Stephan I]] |
| - | [[Category: Beta sandwhich]]
| + | |
| - | [[Category: G-domain]]
| + | |
| - | [[Category: Gtp-binding protein]]
| + | |
| - | [[Category: Immunoglobulin fold]]
| + | |
| - | [[Category: Protein-protein complex]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Walker fold]]
| + | |
| Structural highlights
Disease
RAC2_HUMAN Defects in RAC2 are the cause of neutrophil immunodeficiency syndrome (NEUID) [MIM:608203.[1]
Function
RAC2_HUMAN Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. Augments the production of reactive oxygen species (ROS) by NADPH oxidase.[2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Rho family-specific guanine nucleotide dissociation inhibitors (RhoGDIs) decrease the rate of nucleotide dissociation and release Rho proteins such as RhoA, Rac and Cdc42 from membranes, forming tight complexes that shuttle between cytosol and membrane compartments. We have solved the crystal structure of a complex between the RhoGDI homolog LyGDI and GDP-bound Rac2, which are abundant in leukocytes, representing the cytosolic, resting pool of Rho species to be activated by extracellular signals. The N-terminal domain of LyGDI (LyN), which has been reported to be flexible in isolated RhoGDIs, becomes ordered upon complex formation and contributes more than 60% to the interface area. The structure is consistent with the C-terminus of Rac2 binding to a hydrophobic cavity previously proposed as isoprenyl binding site. An inner segment of LyN forms a helical hairpin that contacts mainly the switch regions of Rac2. The architecture of the complex interface suggests a mechanism for the inhibition of guanine nucleotide dissociation that is based on the stabilization of the magnesium (Mg2+) ion in the nucleotide binding pocket.
The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI.,Scheffzek K, Stephan I, Jensen ON, Illenberger D, Gierschik P Nat Struct Biol. 2000 Feb;7(2):122-6. PMID:10655614[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ambruso DR, Knall C, Abell AN, Panepinto J, Kurkchubasche A, Thurman G, Gonzalez-Aller C, Hiester A, deBoer M, Harbeck RJ, Oyer R, Johnson GL, Roos D. Human neutrophil immunodeficiency syndrome is associated with an inhibitory Rac2 mutation. Proc Natl Acad Sci U S A. 2000 Apr 25;97(9):4654-9. PMID:10758162 doi:10.1073/pnas.080074897
- ↑ Knaus UG, Heyworth PG, Evans T, Curnutte JT, Bokoch GM. Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2. Science. 1991 Dec 6;254(5037):1512-5. PMID:1660188
- ↑ Scheffzek K, Stephan I, Jensen ON, Illenberger D, Gierschik P. The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI. Nat Struct Biol. 2000 Feb;7(2):122-6. PMID:10655614 doi:http://dx.doi.org/10.1038/72392
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