2z0u

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Crystal structure of C2 domain of KIBRA protein

Structural highlights

2z0u 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 2.2Å
Ligands:MSE
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

KIBRA_HUMAN Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with NF2 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. Acts as a transcriptional coactivator of ESR1 which plays an essential role in DYNLL1-mediated ESR1 transactivation. Regulates collagen-stimulated activation of the ERK/MAPK cascade. Modulates directional migration of podocytes. Acts as a substrate for PRKCZ. Plays a role in cognition and memory performance.[1] [2] [3] [4] [5] [6] [7]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. Buther K, Plaas C, Barnekow A, Kremerskothen J. KIBRA is a novel substrate for protein kinase Czeta. Biochem Biophys Res Commun. 2004 May 7;317(3):703-7. PMID:15081397 doi:http://dx.doi.org/10.1016/j.bbrc.2004.03.107
  2. Rayala SK, den Hollander P, Manavathi B, Talukder AH, Song C, Peng S, Barnekow A, Kremerskothen J, Kumar R. Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells. J Biol Chem. 2006 Jul 14;281(28):19092-9. Epub 2006 May 9. PMID:16684779 doi:10.1074/jbc.M600021200
  3. Hilton HN, Stanford PM, Harris J, Oakes SR, Kaplan W, Daly RJ, Ormandy CJ. KIBRA interacts with discoidin domain receptor 1 to modulate collagen-induced signalling. Biochim Biophys Acta. 2008 Mar;1783(3):383-93. doi: 10.1016/j.bbamcr.2007.12.007., Epub 2008 Jan 9. PMID:18190796 doi:http://dx.doi.org/10.1016/j.bbamcr.2007.12.007
  4. Duning K, Schurek EM, Schluter M, Bayer M, Reinhardt HC, Schwab A, Schaefer L, Benzing T, Schermer B, Saleem MA, Huber TB, Bachmann S, Kremerskothen J, Weide T, Pavenstadt H. KIBRA modulates directional migration of podocytes. J Am Soc Nephrol. 2008 Oct;19(10):1891-903. doi: 10.1681/ASN.2007080916. Epub, 2008 Jul 2. PMID:18596123 doi:10.1681/ASN.2007080916
  5. Johannsen S, Duning K, Pavenstadt H, Kremerskothen J, Boeckers TM. Temporal-spatial expression and novel biochemical properties of the memory-related protein KIBRA. Neuroscience. 2008 Sep 9;155(4):1165-73. doi: 10.1016/j.neuroscience.2008.06.054., Epub 2008 Jul 3. PMID:18672031 doi:http://dx.doi.org/10.1016/j.neuroscience.2008.06.054
  6. Yu J, Zheng Y, Dong J, Klusza S, Deng WM, Pan D. Kibra functions as a tumor suppressor protein that regulates Hippo signaling in conjunction with Merlin and Expanded. Dev Cell. 2010 Feb 16;18(2):288-99. doi: 10.1016/j.devcel.2009.12.012. PMID:20159598 doi:http://dx.doi.org/10.1016/j.devcel.2009.12.012
  7. Duning K, Wennmann DO, Bokemeyer A, Reissner C, Wersching H, Thomas C, Buschert J, Guske K, Franzke V, Floel A, Lohmann H, Knecht S, Brand SM, Poter M, Rescher U, Missler M, Seelheim P, Propper C, Boeckers TM, Makuch L, Huganir R, Weide T, Brand E, Pavenstadt H, Kremerskothen J. Common exonic missense variants in the C2 domain of the human KIBRA protein modify lipid binding and cognitive performance. Transl Psychiatry. 2013 Jun 18;3:e272. doi: 10.1038/tp.2013.49. PMID:23778582 doi:http://dx.doi.org/10.1038/tp.2013.49

Contents


PDB ID 2z0u

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