4d0n

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: '''Unreleased structure''' The entry 4d0n is ON HOLD Authors: Abdul Azeez, K.R., Shrestha, L., Krojer, T., Allerston, C., von Delft, F., Bountra, C., Arrowsmith, C., Edwards, A.M., Knap...)
Current revision (11:16, 9 May 2024) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 4d0n is ON HOLD
+
==AKAP13 (AKAP-Lbc) RhoGEF domain in complex with RhoA==
 +
<StructureSection load='4d0n' size='340' side='right'caption='[[4d0n]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[4d0n]] 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=4D0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D0N FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4d0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d0n OCA], [https://pdbe.org/4d0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d0n RCSB], [https://www.ebi.ac.uk/pdbsum/4d0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d0n ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/RHOA_HUMAN RHOA_HUMAN] Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. Stimulates PKN2 kinase activity. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization.<ref>PMID:8910519</ref> <ref>PMID:9121475</ref> <ref>PMID:12900402</ref> <ref>PMID:16103226</ref> <ref>PMID:16236794</ref> <ref>PMID:19934221</ref> <ref>PMID:20937854</ref> <ref>PMID:20974804</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The RhoGEF domain of AKAP-Lbc (AKAP13) catalyses nucleotide exchange on RhoA and is involved in development of cardiac hypertrophy. The RhoGEF activity of AKAP-Lbc has also been implicated in cancer. We have determined the X-ray crystal structure of the complex between RhoA:GDP and the AKAP-Lbc RhoGEF (DH-PH) domain to 2.1 A resolution. The structure reveals important differences compared to related RhoGEF proteins such as Leukemia-associated RhoGEF. Nucleotide exchange assays comparing the activity of the DH-PH domain to the DH domain alone showed no role for the PH domain in nucleotide exchange, which is explained by the RhoA:AKAP-Lbc structure. Comparison to a structure of the isolated AKAP-Lbc DH domain revealed a change in conformation of the N-terminal 'GEF switch' region upon binding to RhoA. Isothermal titration calorimetry showed that AKAP-Lbc has only micromolar affinity for RhoA which combined with the presence of potential binding pockets for small molecules on AKAP-Lbc raises the possibility of targeting AKAP-Lbc with guanine nucleotide exchange factor inhibitors.
-
Authors: Abdul Azeez, K.R., Shrestha, L., Krojer, T., Allerston, C., von Delft, F., Bountra, C., Arrowsmith, C., Edwards, A.M., Knapp, S., Klussmann, E., Elkins, J.M.
+
The Crystal Structure of the RhoA : AKAP-Lbc DH-PH Domain Complex.,Abdul Azeez KR, Knapp S, Fernandes JM, Klussmann E, Elkins JM Biochem J. 2014 Sep 4. PMID:25186459<ref>PMID:25186459</ref>
-
Description: AKAP13 (AKAP-Lbc) RhoGEF domain in complex with RhoA
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 4d0n" style="background-color:#fffaf0;"></div>
 +
 
 +
==See Also==
 +
*[[A-kinase anchor protein 3D structures|A-kinase anchor protein 3D structures]]
 +
*[[Rho GTPase 3D structures|Rho GTPase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Homo sapiens]]
 +
[[Category: Large Structures]]
 +
[[Category: Abdul Azeez KR]]
 +
[[Category: Allerston C]]
 +
[[Category: Arrowsmith C]]
 +
[[Category: Bountra C]]
 +
[[Category: Edwards AM]]
 +
[[Category: Elkins JM]]
 +
[[Category: Klussmann E]]
 +
[[Category: Knapp S]]
 +
[[Category: Krojer T]]
 +
[[Category: Shrestha L]]
 +
[[Category: Von Delft F]]

Current revision

AKAP13 (AKAP-Lbc) RhoGEF domain in complex with RhoA

PDB ID 4d0n

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4d0n"
Personal tools