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1h5p

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Revision as of 06:07, 6 October 2021

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

Structural highlights

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

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^[1]

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

References

↑ 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 Evolutionary Conservation
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='1h5p' size='340' side='right'caption='[[1h5p]], [[NMR_Ensembles_of_Models | 10 NMR models]]' 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/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 [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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h5p ProSAT]</span></td></tr>
+</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>
 == Evolutionary Conservation ==

1h5p

From Proteopedia

Revision as of 06:07, 6 October 2021

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

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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