4nw2

From Proteopedia

(Difference between revisions)

Current revision

Tandem chromodomains of human CHD1 in complex with Influenza virus NS1 C-terminal tail trimethylated at K229

Structural highlights

4nw2 is a 4 chain structure with sequence from Homo sapiens and Influenza A virus (A/swine/Henan/1/2010(H3N2)). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CHD1_HUMAN ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Is also associated with histone deacetylase (HDAC) activity (By similarity). Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing in part through physical bridging of spliceosomal components to H3K4me3. Required for maintaining open chromatin and pluripotency in embryonic stem cells.^[1]

Publication Abstract from PubMed

Pathogens can interfere with vital biological processes of their host by mimicking host proteins. The NS1 protein of the influenza A H3N2 subtype possesses a histone H3K4-like sequence at its carboxyl terminus and has been reported to use this mimic to hijack host proteins. However, this mimic lacks a free N-terminus that is essential for binding to many known H3K4 readers. Here we show that the double chromodomains of CHD1 adopt an 'open pocket' to interact with the free N-terminal amine of H3K4, and the open pocket permits the NS1 mimic to bind in a distinct conformation. We also explored the possibility that NS1 hijacks other cellular proteins and found that the NS1 mimic has access to only a subset of chromatin-associated factors, such as WDR5. Moreover, methylation of the NS1 mimic can not be reversed by the H3K4 demethylase LSD1. Overall, we thus conclude that the NS1 mimic is an imperfect histone mimic.

Structural basis for histone mimicry and hijacking of host proteins by influenza virus protein NS1.,Qin S, Liu Y, Tempel W, Eram MS, Bian C, Liu K, Senisterra G, Crombet L, Vedadi M, Min J Nat Commun. 2014 May 23;5:3952. doi: 10.1038/ncomms4952. PMID:24853335^[2]

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

References

↑ Sims RJ 3rd, Millhouse S, Chen CF, Lewis BA, Erdjument-Bromage H, Tempst P, Manley JL, Reinberg D. Recognition of trimethylated histone H3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing. Mol Cell. 2007 Nov 30;28(4):665-76. PMID:18042460 doi:http://dx.doi.org/10.1016/j.molcel.2007.11.010
↑ Qin S, Liu Y, Tempel W, Eram MS, Bian C, Liu K, Senisterra G, Crombet L, Vedadi M, Min J. Structural basis for histone mimicry and hijacking of host proteins by influenza virus protein NS1. Nat Commun. 2014 May 23;5:3952. doi: 10.1038/ncomms4952. PMID:24853335 doi:http://dx.doi.org/10.1038/ncomms4952

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4nw2"

@@ Line 1: / Line 1: @@
 ==Tandem chromodomains of human CHD1 in complex with Influenza virus NS1 C-terminal tail trimethylated at K229==
-<StructureSection load='4nw2' size='340' side='right' caption='[[4nw2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='4nw2' size='340' side='right'caption='[[4nw2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4nw2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NW2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NW2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4nw2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/swine/Henan/1/2010(H3N2)) Influenza A virus (A/swine/Henan/1/2010(H3N2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NW2 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene><br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CHD1 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=4nw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nw2 OCA], [https://pdbe.org/4nw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nw2 RCSB], [https://www.ebi.ac.uk/pdbsum/4nw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nw2 ProSAT]</span></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nw2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nw2 RCSB], [http://www.ebi.ac.uk/pdbsum/4nw2 PDBsum]</span></td></tr>
+</table>
-<table>
+== Function ==
+[https://www.uniprot.org/uniprot/CHD1_HUMAN CHD1_HUMAN] ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Is also associated with histone deacetylase (HDAC) activity (By similarity). Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing in part through physical bridging of spliceosomal components to H3K4me3. Required for maintaining open chromatin and pluripotency in embryonic stem cells.<ref>PMID:18042460</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 14: / Line 16: @@
 Structural basis for histone mimicry and hijacking of host proteins by influenza virus protein NS1.,Qin S, Liu Y, Tempel W, Eram MS, Bian C, Liu K, Senisterra G, Crombet L, Vedadi M, Min J Nat Commun. 2014 May 23;5:3952. doi: 10.1038/ncomms4952. PMID:24853335<ref>PMID:24853335</ref>
-From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4nw2" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Chromodomain-helicase-DNA-binding protein|Chromodomain-helicase-DNA-binding protein]]
+*[[Chromodomain-helicase-DNA-binding protein 3D structures|Chromodomain-helicase-DNA-binding protein 3D structures]]
-*[[Helicase|Helicase]]
+*[[Helicase 3D structures|Helicase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Arrowsmith, C H.]]
+[[Category: Large Structures]]
-[[Category: Bakkouri, M El.]]
+[[Category: Arrowsmith CH]]
-[[Category: Bountra, C.]]
+[[Category: Bountra C]]
-[[Category: Edwards, A M.]]
+[[Category: Edwards AM]]
-[[Category: Min, J.]]
+[[Category: El Bakkouri M]]
-[[Category: Qin, S.]]
+[[Category: Min J]]
-[[Category: SGC, Structural Genomics Consortium.]]
+[[Category: Qin S]]
-[[Category: Tempel, W.]]
+[[Category: Tempel W]]
-[[Category: Xu, C.]]
+[[Category: Xu C]]
-[[Category: Peptide binding protein-viral protein complex]]
-[[Category: Sgc]]
-[[Category: Structural genomics consortium]]

4nw2

From Proteopedia

Current revision

Tandem chromodomains of human CHD1 in complex with Influenza virus NS1 C-terminal tail trimethylated at K229

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox