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2ell

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Revision as of 06:56, 6 June 2018

Solution structure of the Leucine Rich Repeat of human Acidic leucine-rich nuclear phosphoprotein 32 family member B

Structural highlights

2ell 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.
Gene:	ANP32B (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[AN32B_HUMAN] Multifunctional protein working as a cell cycle progression factor as well as a cell survival factor. Required for the progression from the G1 to the S phase. Anti-apoptotic protein which functions as a caspase-3 inhibitor. Has no phosphatase 2A (PP2A) inhibitor activity (By similarity). Exhibits histone chaperone properties, stimulating core histones to assemble into a nucleosome.^[1]

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

Eukaryotic gene expression is regulated by histone deposition onto and eviction from nucleosomes, which are mediated by several chromatin-modulating factors. Among them, histone chaperones are key factors that facilitate nucleosome assembly. Acidic nuclear phosphoprotein 32B (ANP32B) belongs to the ANP32 family, which shares N-terminal leucine-rich repeats (LRRs) and a C-terminal variable anionic region. The C-terminal region functions as an inhibitor of histone acetylation, but the functional roles of the LRR domain in chromatin regulation have remained elusive. Here, we report that the LRR domain of ANP32B possesses histone chaperone activity and forms a curved structure with a parallel beta-sheet on the concave side and mostly helical elements on the convex side. Our analyses revealed that the interaction of ANP32B with the core histones H3-H4 occurs on its concave side, and both the acidic and hydrophobic residues that compose the concave surface are critical for histone binding. These results provide a structural framework for understanding the functional mechanisms of acidic histone chaperones.

Solution structure of histone chaperone ANP32B: interaction with core histones H3-H4 through its acidic concave domain.,Tochio N, Umehara T, Munemasa Y, Suzuki T, Sato S, Tsuda K, Koshiba S, Kigawa T, Nagai R, Yokoyama S J Mol Biol. 2010 Aug 6;401(1):97-114. Epub 2010 Jun 9. PMID:20538007^[2]

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

References

↑ Tochio N, Umehara T, Munemasa Y, Suzuki T, Sato S, Tsuda K, Koshiba S, Kigawa T, Nagai R, Yokoyama S. Solution structure of histone chaperone ANP32B: interaction with core histones H3-H4 through its acidic concave domain. J Mol Biol. 2010 Aug 6;401(1):97-114. Epub 2010 Jun 9. PMID:20538007 doi:10.1016/j.jmb.2010.06.005
↑ Tochio N, Umehara T, Munemasa Y, Suzuki T, Sato S, Tsuda K, Koshiba S, Kigawa T, Nagai R, Yokoyama S. Solution structure of histone chaperone ANP32B: interaction with core histones H3-H4 through its acidic concave domain. J Mol Biol. 2010 Aug 6;401(1):97-114. Epub 2010 Jun 9. PMID:20538007 doi:10.1016/j.jmb.2010.06.005

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/2ell"

@@ Line 1: / Line 1: @@
 ==Solution structure of the Leucine Rich Repeat of human Acidic leucine-rich nuclear phosphoprotein 32 family member B==
 <StructureSection load='2ell' size='340' side='right' caption='[[2ell]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[2ell]] 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=2ELL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ELL FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ANP32B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2ell FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ell OCA], [http://pdbe.org/2ell PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ell RCSB], [http://www.ebi.ac.uk/pdbsum/2ell PDBsum], [http://www.topsan.org/Proteins/RSGI/2ell TOPSAN]</span></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=2ell FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ell OCA], [http://pdbe.org/2ell PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ell RCSB], [http://www.ebi.ac.uk/pdbsum/2ell PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ell ProSAT], [http://www.topsan.org/Proteins/RSGI/2ell TOPSAN]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/el/2ell_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/el/2ell_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2ell

From Proteopedia

Revision as of 06:56, 6 June 2018

Solution structure of the Leucine Rich Repeat of human Acidic leucine-rich nuclear phosphoprotein 32 family member B

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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