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| | <StructureSection load='6d4g' size='340' side='right'caption='[[6d4g]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='6d4g' size='340' side='right'caption='[[6d4g]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6d4g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D4G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D4G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6d4g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D4G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6D4G FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</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]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3c5h|3c5h]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Arhgap35, Grlf1, P190A, p190ARHOGAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=6d4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d4g OCA], [https://pdbe.org/6d4g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6d4g RCSB], [https://www.ebi.ac.uk/pdbsum/6d4g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6d4g ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6d4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d4g OCA], [http://pdbe.org/6d4g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d4g RCSB], [http://www.ebi.ac.uk/pdbsum/6d4g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d4g ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RHG35_RAT RHG35_RAT]] Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'. May transduce signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP). May also act as a tumor suppressor (By similarity). | + | [https://www.uniprot.org/uniprot/RHG35_RAT RHG35_RAT] Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'. May transduce signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP). May also act as a tumor suppressor (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Boggon, T J]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Stiegler, A L]] | + | [[Category: Boggon TJ]] |
| - | [[Category: Gtp]] | + | [[Category: Stiegler AL]] |
| - | [[Category: Gtpase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: P190rhogap]]
| + | |
| - | [[Category: Pseudogtpase]]
| + | |
| Structural highlights
Function
RHG35_RAT Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'. May transduce signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP). May also act as a tumor suppressor (By similarity).
Publication Abstract from PubMed
The pseudoGTPases are a rapidly growing and important group of pseudoenzymes. p190RhoGAP proteins are critical regulators of Rho signaling and contain two previously identified pseudoGTPase domains. Here we report that p190RhoGAP proteins contain a third pseudoGTPase domain, termed N-GTPase. We find that GTP constitutively purifies with the N-GTPase domain, and a 2.8-A crystal structure of p190RhoGAP-A co-purified with GTP reveals an unusual GTP-Mg(2+) binding pocket. Six inserts in N-GTPase indicate perturbed catalytic activity and inability to bind to canonical GTPase activating proteins, guanine nucleotide exchange factors, and effector proteins. Biochemical analysis shows that N-GTPase does not detectably hydrolyze GTP, and exchanges nucleotide only under harsh Mg(2+) chelation. Furthermore, mutational analysis shows that GTP and Mg(2+) binding stabilizes the domain. Therefore, our results support that N-GTPase is a nucleotide binding, non-hydrolyzing, pseudoGTPase domain that may act as a protein-protein interaction domain. Thus, unique among known proteins, p190RhoGAPs contain three pseudoGTPase domains.
The N-Terminal GTPase Domain of p190RhoGAP Proteins Is a PseudoGTPase.,Stiegler AL, Boggon TJ Structure. 2018 Aug 16. pii: S0969-2126(18)30261-2. doi:, 10.1016/j.str.2018.07.015. PMID:30174148[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stiegler AL, Boggon TJ. The N-Terminal GTPase Domain of p190RhoGAP Proteins Is a PseudoGTPase. Structure. 2018 Aug 16. pii: S0969-2126(18)30261-2. doi:, 10.1016/j.str.2018.07.015. PMID:30174148 doi:http://dx.doi.org/10.1016/j.str.2018.07.015
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