1h5p

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of the human Sp100b SAND domain by heteronuclear NMR.

Structural highlights

1h5p is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SP100_HUMAN Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2 according to PubMed:11909962. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA according to PubMed:15247905. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53-mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. Also plays a role in infection by viruses, including human cytomegalovirus and Epstein-Barr virus, through mechanisms that may involve chromatin and/or transcriptional regulation.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9]

Evolutionary Conservation

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

Publication Abstract from PubMed

The SAND domain is a conserved sequence motif found in a number of nuclear proteins, including the Sp100 family and NUDR. These are thought to play important roles in chromatin-dependent transcriptional regulation and are linked to many diseases. We have determined the three-dimensional (3D) structure of the SAND domain from Sp100b. The structure represents a novel alpha/beta fold, in which a conserved KDWK sequence motif is found within an alpha-helical, positively charged surface patch. For NUDR, the SAND domain is shown to be sufficient to mediate DNA binding. Using mutational analyses and chemical shift perturbation experiments, the DNA binding surface is mapped to the alpha-helical region encompassing the KDWK motif. The DNA binding activity of wild type and mutant proteins in vitro correlates with transcriptional regulation activity of full length NUDR in vivo. The evolutionarily conserved SAND domain defines a new DNA binding fold that is involved in chromatin-associated transcriptional regulation.

The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation.,Bottomley MJ, Collard MW, Huggenvik JI, Liu Z, Gibson TJ, Sattler M Nat Struct Biol. 2001 Jul;8(7):626-33. PMID:11427895^[10]

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

References

↑ Wasylyk C, Schlumberger SE, Criqui-Filipe P, Wasylyk B. Sp100 interacts with ETS-1 and stimulates its transcriptional activity. Mol Cell Biol. 2002 Apr;22(8):2687-702. PMID:11909962
↑ Moller A, Sirma H, Hofmann TG, Staege H, Gresko E, Ludi KS, Klimczak E, Droge W, Will H, Schmitz ML. Sp100 is important for the stimulatory effect of homeodomain-interacting protein kinase-2 on p53-dependent gene expression. Oncogene. 2003 Nov 27;22(54):8731-7. PMID:14647468 doi:http://dx.doi.org/10.1038/sj.onc.1207079
↑ Yordy JS, Li R, Sementchenko VI, Pei H, Muise-Helmericks RC, Watson DK. SP100 expression modulates ETS1 transcriptional activity and inhibits cell invasion. Oncogene. 2004 Aug 26;23(39):6654-65. PMID:15247905 doi:http://dx.doi.org/10.1038/sj.onc.1207891
↑ Yordy JS, Moussa O, Pei H, Chaussabel D, Li R, Watson DK. SP100 inhibits ETS1 activity in primary endothelial cells. Oncogene. 2005 Jan 27;24(5):916-31. PMID:15592518 doi:http://dx.doi.org/10.1038/sj.onc.1208245
↑ Jiang WQ, Zhong ZH, Henson JD, Neumann AA, Chang AC, Reddel RR. Suppression of alternative lengthening of telomeres by Sp100-mediated sequestration of the MRE11/RAD50/NBS1 complex. Mol Cell Biol. 2005 Apr;25(7):2708-21. PMID:15767676 doi:http://dx.doi.org/10.1128/MCB.25.7.2708-2721.2005
↑ Ling PD, Peng RS, Nakajima A, Yu JH, Tan J, Moses SM, Yang WH, Zhao B, Kieff E, Bloch KD, Bloch DB. Mediation of Epstein-Barr virus EBNA-LP transcriptional coactivation by Sp100. EMBO J. 2005 Oct 19;24(20):3565-75. Epub 2005 Sep 22. PMID:16177824 doi:http://dx.doi.org/7600820
↑ Milovic-Holm K, Krieghoff E, Jensen K, Will H, Hofmann TG. FLASH links the CD95 signaling pathway to the cell nucleus and nuclear bodies. EMBO J. 2007 Jan 24;26(2):391-401. PMID:17245429 doi:http://dx.doi.org/10.1038/sj.emboj.7601504
↑ Held-Feindt J, Hattermann K, Knerlich-Lukoschus F, Mehdorn HM, Mentlein R. SP100 reduces malignancy of human glioma cells. Int J Oncol. 2011 Apr;38(4):1023-30. doi: 10.3892/ijo.2011.927. Epub 2011 Jan 27. PMID:21274506 doi:http://dx.doi.org/10.3892/ijo.2011.927
↑ Kim YE, Lee JH, Kim ET, Shin HJ, Gu SY, Seol HS, Ling PD, Lee CH, Ahn JH. Human cytomegalovirus infection causes degradation of Sp100 proteins that suppress viral gene expression. J Virol. 2011 Nov;85(22):11928-37. doi: 10.1128/JVI.00758-11. Epub 2011 Aug 31. PMID:21880768 doi:http://dx.doi.org/10.1128/JVI.00758-11
↑ Bottomley MJ, Collard MW, Huggenvik JI, Liu Z, Gibson TJ, Sattler M. The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation. Nat Struct Biol. 2001 Jul;8(7):626-33. PMID:11427895 doi:http://dx.doi.org/10.1038/89675

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1h5p"

@@ Line 1: / Line 1: @@
-==SOLUTION STRUCTURE OF THE HUMAN SP100B SAND DOMAIN BY HETERONUCLEAR NMR.==
-<StructureSection load='1h5p' size='340' side='right' caption='[[1h5p]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+==Solution structure of the human Sp100b SAND domain by heteronuclear NMR.==
+<StructureSection load='1h5p' size='340' side='right'caption='[[1h5p]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1h5p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H5P FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1h5p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H5P FirstGlance]. <br>
-</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=1h5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5p OCA], [http://pdbe.org/1h5p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h5p RCSB], [http://www.ebi.ac.uk/pdbsum/1h5p PDBsum]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1h5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5p OCA], [https://pdbe.org/1h5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h5p RCSB], [https://www.ebi.ac.uk/pdbsum/1h5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h5p ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SP100_HUMAN SP100_HUMAN] Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2 according to PubMed:11909962. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA according to PubMed:15247905. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53-mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. Also plays a role in infection by viruses, including human cytomegalovirus and Epstein-Barr virus, through mechanisms that may involve chromatin and/or transcriptional regulation.<ref>PMID:11909962</ref> <ref>PMID:14647468</ref> <ref>PMID:15247905</ref> <ref>PMID:15592518</ref> <ref>PMID:15767676</ref> <ref>PMID:16177824</ref> <ref>PMID:17245429</ref> <ref>PMID:21274506</ref> <ref>PMID:21880768</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h5/1h5p_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h5/1h5p_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h5p ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Bottomley, M J]]
+[[Category: Large Structures]]
-[[Category: Collard, M W]]
+[[Category: Bottomley MJ]]
-[[Category: Gibson, T J]]
+[[Category: Collard MW]]
-[[Category: Huggenvik, J I]]
+[[Category: Gibson TJ]]
-[[Category: Liu, Z]]
+[[Category: Huggenvik JI]]
-[[Category: Sattler, M]]
+[[Category: Liu Z]]
-[[Category: Antigen]]
+[[Category: Sattler M]]
-[[Category: Dna binding]]
-[[Category: Kdwk]]
-[[Category: Nuclear protein]]
-[[Category: Sand domain]]
-[[Category: Sp100b]]
-[[Category: Transcription]]

1h5p

From Proteopedia

Current revision

Solution structure of the human Sp100b SAND domain by heteronuclear NMR.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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