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| | ==ANP32A LRR domain== | | ==ANP32A LRR domain== |
| - | <StructureSection load='4xos' size='340' side='right' caption='[[4xos]], [[Resolution|resolution]] 1.56Å' scene=''> | + | <StructureSection load='4xos' size='340' side='right'caption='[[4xos]], [[Resolution|resolution]] 1.56Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xos]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XOS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XOS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xos]] 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=4XOS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XOS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 1.559Å</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=4xos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xos OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xos RCSB], [http://www.ebi.ac.uk/pdbsum/4xos PDBsum]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4xos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xos OCA], [https://pdbe.org/4xos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xos RCSB], [https://www.ebi.ac.uk/pdbsum/4xos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xos ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AN32A_HUMAN AN32A_HUMAN]] Implicated in a number of cellular processes, including proliferation, differentiation, caspase-dependent and caspase-independent apoptosis, suppression of transformation (tumor suppressor), inhibition of protein phosphatase 2A, regulation of mRNA trafficking and stability in association with ELAVL1, and inhibition of acetyltransferases as part of the INHAT (inhibitor of histone acetyltransferases) complex. Plays a role in E4F1-mediated transcriptional repression.<ref>PMID:15642345</ref> <ref>PMID:10400610</ref> <ref>PMID:11360199</ref> <ref>PMID:17557114</ref> | + | [https://www.uniprot.org/uniprot/AN32A_HUMAN AN32A_HUMAN] Implicated in a number of cellular processes, including proliferation, differentiation, caspase-dependent and caspase-independent apoptosis, suppression of transformation (tumor suppressor), inhibition of protein phosphatase 2A, regulation of mRNA trafficking and stability in association with ELAVL1, and inhibition of acetyltransferases as part of the INHAT (inhibitor of histone acetyltransferases) complex. Plays a role in E4F1-mediated transcriptional repression.<ref>PMID:15642345</ref> <ref>PMID:10400610</ref> <ref>PMID:11360199</ref> <ref>PMID:17557114</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4xos" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bravo, J]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Zamora-Caballero, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Antitumor protein]] | + | [[Category: Bravo J]] |
| - | [[Category: Component of the set complex]] | + | [[Category: Zamora-Caballero S]] |
| - | [[Category: Leucine rich repeat tumor suppressor]]
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| Structural highlights
Function
AN32A_HUMAN Implicated in a number of cellular processes, including proliferation, differentiation, caspase-dependent and caspase-independent apoptosis, suppression of transformation (tumor suppressor), inhibition of protein phosphatase 2A, regulation of mRNA trafficking and stability in association with ELAVL1, and inhibition of acetyltransferases as part of the INHAT (inhibitor of histone acetyltransferases) complex. Plays a role in E4F1-mediated transcriptional repression.[1] [2] [3] [4]
Publication Abstract from PubMed
Acidic leucine-rich nuclear phosphoprotein 32A (PP32A) is a tumour suppressor whose expression is altered in many cancers. It is an apoptotic enhancer that stimulates apoptosome-mediated caspase activation and also forms part of a complex involved in caspase-independent apoptosis (the SET complex). Crystals of a fragment of human PP32A corresponding to the leucine-rich repeat domain, a widespread motif suitable for protein-protein interactions, have been obtained. The structure has been refined to 1.56 A resolution. This domain was previously solved at 2.4 and 2.69 A resolution (PDB entries 2je0 and 2je1, respectively). The new high-resolution structure shows some differences from previous models: there is a small displacement in the turn connecting the first alpha-helix (alpha1) to the first beta-strand (beta1), which slightly changes the position of alpha1 in the structure. The shift in the turn is observed in the context of a new crystal packing unrelated to those of previous structures.
High-resolution crystal structure of the leucine-rich repeat domain of the human tumour suppressor PP32A (ANP32A).,Zamora-Caballero S, Siauciunaite-Gaubard L, Bravo J Acta Crystallogr F Struct Biol Commun. 2015 Jun 1;71(Pt 6):684-7. doi:, 10.1107/S2053230X15006457. Epub 2015 May 20. PMID:26057796[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tsujio I, Zaidi T, Xu J, Kotula L, Grundke-Iqbal I, Iqbal K. Inhibitors of protein phosphatase-2A from human brain structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated tau. FEBS Lett. 2005 Jan 17;579(2):363-72. PMID:15642345 doi:http://dx.doi.org/S0014-5793(04)01509-1
- ↑ Brody JR, Kadkol SS, Mahmoud MA, Rebel JM, Pasternack GR. Identification of sequences required for inhibition of oncogene-mediated transformation by pp32. J Biol Chem. 1999 Jul 16;274(29):20053-5. PMID:10400610
- ↑ Bai J, Brody JR, Kadkol SS, Pasternack GR. Tumor suppression and potentiation by manipulation of pp32 expression. Oncogene. 2001 Apr 19;20(17):2153-60. PMID:11360199 doi:http://dx.doi.org/10.1038/sj.onc.1204294
- ↑ Cvetanovic M, Rooney RJ, Garcia JJ, Toporovskaya N, Zoghbi HY, Opal P. The role of LANP and ataxin 1 in E4F-mediated transcriptional repression. EMBO Rep. 2007 Jul;8(7):671-7. Epub 2007 Jun 8. PMID:17557114 doi:http://dx.doi.org/7400983
- ↑ Zamora-Caballero S, Siauciunaite-Gaubard L, Bravo J. High-resolution crystal structure of the leucine-rich repeat domain of the human tumour suppressor PP32A (ANP32A). Acta Crystallogr F Struct Biol Commun. 2015 Jun 1;71(Pt 6):684-7. doi:, 10.1107/S2053230X15006457. Epub 2015 May 20. PMID:26057796 doi:http://dx.doi.org/10.1107/S2053230X15006457
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