7av9: Difference between revisions

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New page: '''Unreleased structure''' The entry 7av9 is ON HOLD Authors: Krojer, T., Talon, R., Fairhead, M., Szykowska, A., Burgess-Brown, N.A., Brennan, P.E., Arrowsmith, C.H., Edwards, A.M., Bo...
 
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'''Unreleased structure'''


The entry 7av9 is ON HOLD
==Crystal Structure of the second bromodomain of Pleckstrin homology domain interacting protein (PHIP) in space group C2==
<StructureSection load='7av9' size='340' side='right'caption='[[7av9]], [[Resolution|resolution]] 1.23&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7av9]] is a 1 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=7AV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AV9 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]] 1.23&#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></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=7av9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7av9 OCA], [https://pdbe.org/7av9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7av9 RCSB], [https://www.ebi.ac.uk/pdbsum/7av9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7av9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHIP_HUMAN PHIP_HUMAN] Probable regulator of the insulin and insulin-like growth factor signaling pathways. Stimulates cell proliferation through regulation of cyclin transcription and has an anti-apoptotic activity through AKT1 phosphorylation and activation. Plays a role in the regulation of cell morphology and cytoskeletal organization.<ref>PMID:12242307</ref> <ref>PMID:21834987</ref>


Authors: Krojer, T., Talon, R., Fairhead, M., Szykowska, A., Burgess-Brown, N.A., Brennan, P.E., Arrowsmith, C.H., Edwards, A.M., Bountra, C., von Delft, F.
==See Also==
 
*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]]
Description: Crystal Structure of the second bromodomain of Pleckstrin homology domain interacting protein (PHIP) in space group C2
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Burgess-Brown, N.A]]
__TOC__
[[Category: Fairhead, M]]
</StructureSection>
[[Category: Krojer, T]]
[[Category: Homo sapiens]]
[[Category: Bountra, C]]
[[Category: Large Structures]]
[[Category: Szykowska, A]]
[[Category: Arrowsmith CH]]
[[Category: Edwards, A.M]]
[[Category: Bountra C]]
[[Category: Talon, R]]
[[Category: Brennan PE]]
[[Category: Brennan, P.E]]
[[Category: Burgess-Brown NA]]
[[Category: Arrowsmith, C.H]]
[[Category: Edwards AM]]
[[Category: Von Delft, F]]
[[Category: Fairhead M]]
[[Category: Krojer T]]
[[Category: Szykowska A]]
[[Category: Talon R]]
[[Category: Von Delft F]]

Latest revision as of 15:16, 1 February 2024

Crystal Structure of the second bromodomain of Pleckstrin homology domain interacting protein (PHIP) in space group C2Crystal Structure of the second bromodomain of Pleckstrin homology domain interacting protein (PHIP) in space group C2

Structural highlights

7av9 is a 1 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 1.23Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PHIP_HUMAN Probable regulator of the insulin and insulin-like growth factor signaling pathways. Stimulates cell proliferation through regulation of cyclin transcription and has an anti-apoptotic activity through AKT1 phosphorylation and activation. Plays a role in the regulation of cell morphology and cytoskeletal organization.[1] [2]

See Also

References

  1. Farhang-Fallah J, Randhawa VK, Nimnual A, Klip A, Bar-Sagi D, Rozakis-Adcock M. The pleckstrin homology (PH) domain-interacting protein couples the insulin receptor substrate 1 PH domain to insulin signaling pathways leading to mitogenesis and GLUT4 translocation. Mol Cell Biol. 2002 Oct;22(20):7325-36. PMID:12242307
  2. Bai SW, Herrera-Abreu MT, Rohn JL, Racine V, Tajadura V, Suryavanshi N, Bechtel S, Wiemann S, Baum B, Ridley AJ. Identification and characterization of a set of conserved and new regulators of cytoskeletal organization, cell morphology and migration. BMC Biol. 2011 Aug 11;9:54. doi: 10.1186/1741-7007-9-54. PMID:21834987 doi:10.1186/1741-7007-9-54

7av9, resolution 1.23Å

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OCA