2ma2: Difference between revisions

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==Solution structure of RasGRP2 EF hands bound to calcium==
==Solution structure of RasGRP2 EF hands bound to calcium==
<StructureSection load='2ma2' size='340' side='right' caption='[[2ma2]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='2ma2' size='340' side='right'caption='[[2ma2]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ma2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MA2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MA2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ma2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MA2 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l9m|4l9m]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RASGRP2, CDC25L, MCG7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2ma2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ma2 OCA], [https://pdbe.org/2ma2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ma2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ma2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ma2 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=2ma2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ma2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ma2 RCSB], [http://www.ebi.ac.uk/pdbsum/2ma2 PDBsum]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/GRP2_HUMAN GRP2_HUMAN] Functions as a calcium- and DAG-regulated nucleotide exchange factor specifically activating Rap through the exchange of bound GDP for GTP. May also activates other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. Functions in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation. May function in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway.<ref>PMID:10918068</ref> <ref>PMID:14702343</ref> <ref>PMID:17702895</ref> <ref>PMID:17576779</ref>  
RasGRP1 and SOS are Ras-specific nucleotide exchange factors that have distinct roles in lymphocyte development. RasGRP1 is important in some cancers and autoimmune diseases but, in contrast to SOS, its regulatory mechanisms are poorly understood. Activating signals lead to the membrane recruitment of RasGRP1 and Ras engagement, but it is unclear how interactions between RasGRP1 and Ras are suppressed in the absence of such signals. We present a crystal structure of a fragment of RasGRP1 in which the Ras-binding site is blocked by an interdomain linker and the membrane-interaction surface of RasGRP1 is hidden within a dimerization interface that may be stabilized by the C-terminal oligomerization domain. NMR data demonstrate that calcium binding to the regulatory module generates substantial conformational changes that are incompatible with the inactive assembly. These features allow RasGRP1 to be maintained in an inactive state that is poised for activation by calcium and membrane-localization signals. DOI:http://dx.doi.org/10.7554/eLife.00813.001.
 
Structural analysis of autoinhibition in the Ras-specific exchange factor RasGRP1.,Iwig JS, Vercoulen Y, Das R, Barros T, Limnander A, Che Y, Pelton JG, Wemmer DE, Roose JP, Kuriyan J Elife. 2013 Jul 30;2:e00813. doi: 10.7554/eLife.00813. Print 2013. PMID:23908768<ref>PMID:23908768</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Barros, T]]
[[Category: Large Structures]]
[[Category: Che, Y]]
[[Category: Barros T]]
[[Category: Das, R]]
[[Category: Che Y]]
[[Category: Iwig, J]]
[[Category: Das R]]
[[Category: Kuriyan, J]]
[[Category: Iwig J]]
[[Category: Limnander, A]]
[[Category: Kuriyan J]]
[[Category: Pelton, J]]
[[Category: Limnander A]]
[[Category: Roose, J]]
[[Category: Pelton J]]
[[Category: Vercoulen, Y]]
[[Category: Roose J]]
[[Category: Wemmer, D]]
[[Category: Vercoulen Y]]
[[Category: Calcium-binding protein]]
[[Category: Wemmer D]]
[[Category: Ef hand]]
[[Category: Protein]]

Latest revision as of 06:59, 1 May 2024

Solution structure of RasGRP2 EF hands bound to calcium

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