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==Structure of the cGMP Dependent Protein Kinase II and Rab11b Complex== | ==Structure of the cGMP Dependent Protein Kinase II and Rab11b Complex== | ||
<StructureSection load='4ojk' size='340' side='right' caption='[[4ojk]], [[Resolution|resolution]] 2.66Å' scene=''> | <StructureSection load='4ojk' size='340' side='right'caption='[[4ojk]], [[Resolution|resolution]] 2.66Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ojk]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OJK OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4ojk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OJK FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.657Å</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></td></tr> | |||
<tr><td class="sblockLbl"><b> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ojk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ojk OCA], [https://pdbe.org/4ojk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ojk RCSB], [https://www.ebi.ac.uk/pdbsum/4ojk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ojk ProSAT]</span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </table> | ||
<table> | == Function == | ||
[https://www.uniprot.org/uniprot/RB11B_HUMAN RB11B_HUMAN] GTPase that modulates endosomal trafficking. Acts as a major regulator of membrane delivery during cytokinesis (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
cGMP-dependent protein kinase (PKG)-interacting proteins (GKIPs) mediate cellular targeting of PKG isoforms by interacting with their leucine zipper (LZ) domains. These interactions prevent aberrant signaling cross-talk between different PKG isotypes. To gain detailed insight into isotype-specific GKIP recognition by PKG, we analyzed the type II PKG leucine zipper domain and found that residues 40-83 dimerized and specifically interacted with Rab11b. Next, we determined a crystal structure of the PKG II LZ-Rab11b complex. The PKG II LZ domain presents a mostly nonpolar surface onto which Rab11b docks, through van der Waals interactions. Contact surfaces in Rab11b are found in switch I and II, interswitch, and the beta1/N-terminal regions. This binding surface dramatically differs from that seen in the Rab11 family of interacting protein complex structures. Structural comparison with PKG Ialpha and Ibeta LZs combined with mutagenic analysis reveals that GKIP recognition is mediated through surface charge interactions. | |||
Crystal Structure of the cGMP-dependent Protein Kinase II Leucine Zipper and Rab11b Protein Complex Reveals Molecular Details of G-kinase-specific Interactions.,Reger AS, Yang MP, Koide-Yoshida S, Guo E, Mehta S, Yuasa K, Liu A, Casteel DE, Kim C J Biol Chem. 2014 Sep 12;289(37):25393-403. doi: 10.1074/jbc.M114.575894. Epub, 2014 Jul 28. PMID:25070890<ref>PMID:25070890</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4ojk" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rattus norvegicus]] | ||
[[Category: | [[Category: Guo E]] | ||
[[Category: | [[Category: Kim C]] | ||
[[Category: | [[Category: Reger AS]] | ||
[[Category: | [[Category: Yang MP]] | ||
Latest revision as of 20:15, 20 September 2023
Structure of the cGMP Dependent Protein Kinase II and Rab11b ComplexStructure of the cGMP Dependent Protein Kinase II and Rab11b Complex
Structural highlights
FunctionRB11B_HUMAN GTPase that modulates endosomal trafficking. Acts as a major regulator of membrane delivery during cytokinesis (By similarity). Publication Abstract from PubMedcGMP-dependent protein kinase (PKG)-interacting proteins (GKIPs) mediate cellular targeting of PKG isoforms by interacting with their leucine zipper (LZ) domains. These interactions prevent aberrant signaling cross-talk between different PKG isotypes. To gain detailed insight into isotype-specific GKIP recognition by PKG, we analyzed the type II PKG leucine zipper domain and found that residues 40-83 dimerized and specifically interacted with Rab11b. Next, we determined a crystal structure of the PKG II LZ-Rab11b complex. The PKG II LZ domain presents a mostly nonpolar surface onto which Rab11b docks, through van der Waals interactions. Contact surfaces in Rab11b are found in switch I and II, interswitch, and the beta1/N-terminal regions. This binding surface dramatically differs from that seen in the Rab11 family of interacting protein complex structures. Structural comparison with PKG Ialpha and Ibeta LZs combined with mutagenic analysis reveals that GKIP recognition is mediated through surface charge interactions. Crystal Structure of the cGMP-dependent Protein Kinase II Leucine Zipper and Rab11b Protein Complex Reveals Molecular Details of G-kinase-specific Interactions.,Reger AS, Yang MP, Koide-Yoshida S, Guo E, Mehta S, Yuasa K, Liu A, Casteel DE, Kim C J Biol Chem. 2014 Sep 12;289(37):25393-403. doi: 10.1074/jbc.M114.575894. Epub, 2014 Jul 28. PMID:25070890[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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