1m7b: Difference between revisions

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==Crystal structure of Rnd3/RhoE: functional implications==
==Crystal structure of Rnd3/RhoE: functional implications==
<StructureSection load='1m7b' size='340' side='right' caption='[[1m7b]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1m7b' size='340' side='right' caption='[[1m7b]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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</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='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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rnd3 (amino acids 19-200) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rnd3 (amino acids 19-200) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1m7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7b OCA], [http://pdbe.org/1m7b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m7b RCSB], [http://www.ebi.ac.uk/pdbsum/1m7b PDBsum]</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=1m7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7b OCA], [http://pdbe.org/1m7b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m7b RCSB], [http://www.ebi.ac.uk/pdbsum/1m7b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m7b ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m7b ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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==See Also==
==See Also==
*[[GTP-binding protein|GTP-binding protein]]
*[[Rho GTPase|Rho GTPase]]
== References ==
== References ==
<references/>
<references/>

Revision as of 13:37, 18 October 2017

Crystal structure of Rnd3/RhoE: functional implicationsCrystal structure of Rnd3/RhoE: functional implications

Structural highlights

1m7b is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:Rnd3 (amino acids 19-200) (HUMAN)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RND3_HUMAN] Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins.

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

The Rnd proteins constitute an exceptional subfamily within the Rho GTPase family. They possess extended chains at both termini and four prominent amino acid deviations causing GTPase deficiency. Herein, we report the crystal structure of the Rnd3/RhoE G-domain (amino acids 19-200) at 2.0 A resolution. This is the first GTP-structure of a Rho family member which reveals a similar fold but striking differences from RhoA concerning (i) GTPase center, (ii) charge distribution at several surface areas, (iii) C3-transferase binding site and (iv) interacting interfaces towards RhoA regulators and effectors.

Crystal structure of Rnd3/RhoE: functional implications.,Fiegen D, Blumenstein L, Stege P, Vetter IR, Ahmadian MR FEBS Lett. 2002 Aug 14;525(1-3):100-4. PMID:12163169[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Fiegen D, Blumenstein L, Stege P, Vetter IR, Ahmadian MR. Crystal structure of Rnd3/RhoE: functional implications. FEBS Lett. 2002 Aug 14;525(1-3):100-4. PMID:12163169

1m7b, resolution 2.00Å

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