4d0o: Difference between revisions

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==AKAP13 (AKAP-Lbc) DH domain==
==AKAP13 (AKAP-Lbc) DH domain==
<StructureSection load='4d0o' size='340' side='right' caption='[[4d0o]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
<StructureSection load='4d0o' size='340' side='right'caption='[[4d0o]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4d0o]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D0O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D0O FirstGlance]. <br>
<table><tr><td colspan='2'>[[4d0o]] 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=4D0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D0O FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d0n|4d0n]]</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]] 2.75&#8491;</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=4d0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d0o OCA], [http://pdbe.org/4d0o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d0o RCSB], [http://www.ebi.ac.uk/pdbsum/4d0o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d0o ProSAT]</span></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=4d0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d0o OCA], [https://pdbe.org/4d0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d0o RCSB], [https://www.ebi.ac.uk/pdbsum/4d0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d0o ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/AKP13_HUMAN AKP13_HUMAN]] Anchors cAMP-dependent protein kinase (PKA) and acts as an adapter protein to selectively couple G alpha-13 and Rho. Augments gene activation by the estrogen receptor in an element-specific and ligand-dependent manner. Activates estrogen receptor beta by a p38 MAPK-dependent pathway. Stimulates exchange activity on Rho proteins in vitro, but not on CDC42, Ras or Rac and may bind calcium ions.<ref>PMID:11546812</ref> <ref>PMID:9627117</ref> <ref>PMID:9891067</ref> <ref>PMID:11579095</ref>
[https://www.uniprot.org/uniprot/AKP13_HUMAN AKP13_HUMAN] Anchors cAMP-dependent protein kinase (PKA) and acts as an adapter protein to selectively couple G alpha-13 and Rho. Augments gene activation by the estrogen receptor in an element-specific and ligand-dependent manner. Activates estrogen receptor beta by a p38 MAPK-dependent pathway. Stimulates exchange activity on Rho proteins in vitro, but not on CDC42, Ras or Rac and may bind calcium ions.<ref>PMID:11546812</ref> <ref>PMID:9627117</ref> <ref>PMID:9891067</ref> <ref>PMID:11579095</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4d0o" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4d0o" style="background-color:#fffaf0;"></div>
==See Also==
*[[A-kinase anchor protein 3D structures|A-kinase anchor protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Allerston, C]]
[[Category: Homo sapiens]]
[[Category: Arrowsmith, C]]
[[Category: Large Structures]]
[[Category: Azeez, K R.Abdul]]
[[Category: Abdul Azeez KR]]
[[Category: Bountra, C]]
[[Category: Allerston C]]
[[Category: Delft, F von]]
[[Category: Arrowsmith C]]
[[Category: Edwards, A M]]
[[Category: Bountra C]]
[[Category: Elkins, J M]]
[[Category: Edwards AM]]
[[Category: Klussmann, E]]
[[Category: Elkins JM]]
[[Category: Knapp, S]]
[[Category: Klussmann E]]
[[Category: Krojer, T]]
[[Category: Knapp S]]
[[Category: Shrestha, L]]
[[Category: Krojer T]]
[[Category: Akap-lbc]]
[[Category: Shrestha L]]
[[Category: Cell cycle]]
[[Category: Von Delft F]]
[[Category: Gef]]
[[Category: Ph domain]]
[[Category: Rhogef]]

Latest revision as of 14:16, 9 May 2024

AKAP13 (AKAP-Lbc) DH domainAKAP13 (AKAP-Lbc) DH domain

Structural highlights

4d0o is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.75Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AKP13_HUMAN Anchors cAMP-dependent protein kinase (PKA) and acts as an adapter protein to selectively couple G alpha-13 and Rho. Augments gene activation by the estrogen receptor in an element-specific and ligand-dependent manner. Activates estrogen receptor beta by a p38 MAPK-dependent pathway. Stimulates exchange activity on Rho proteins in vitro, but not on CDC42, Ras or Rac and may bind calcium ions.[1] [2] [3] [4]

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.

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[5]

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

See Also

References

  1. ↑ Diviani D, Soderling J, Scott JD. AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation. J Biol Chem. 2001 Nov 23;276(47):44247-57. Epub 2001 Sep 6. PMID:11546812 doi:http://dx.doi.org/10.1074/jbc.M106629200
  2. ↑ Rubino D, Driggers P, Arbit D, Kemp L, Miller B, Coso O, Pagliai K, Gray K, Gutkind S, Segars J. Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action. Oncogene. 1998 May 14;16(19):2513-26. PMID:9627117 doi:http://dx.doi.org/10.1038/sj.onc.1201783
  3. ↑ Sterpetti P, Hack AA, Bashar MP, Park B, Cheng SD, Knoll JH, Urano T, Feig LA, Toksoz D. Activation of the Lbc Rho exchange factor proto-oncogene by truncation of an extended C terminus that regulates transformation and targeting. Mol Cell Biol. 1999 Feb;19(2):1334-45. PMID:9891067
  4. ↑ Driggers PH, Segars JH, Rubino DM. The proto-oncoprotein Brx activates estrogen receptor beta by a p38 mitogen-activated protein kinase pathway. J Biol Chem. 2001 Dec 14;276(50):46792-7. Epub 2001 Sep 28. PMID:11579095 doi:http://dx.doi.org/10.1074/jbc.M106927200
  5. ↑ Abdul Azeez KR, Knapp S, Fernandes JM, Klussmann E, Elkins JM. The Crystal Structure of the RhoA : AKAP-Lbc DH-PH Domain Complex. Biochem J. 2014 Sep 4. PMID:25186459 doi:http://dx.doi.org/10.1042/BJ20140606

4d0o, resolution 2.75Å

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