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PDBsum entry 6v2s

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protein ligands Protein-protein interface(s) links
Gene regulation PDB id
6v2s

 

 

 

 

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Contents
Protein chains
60 a.a.
Ligands
5R0-PHE-ALA-LEU-
ELY-5R5
×2
UNX ×19
Waters ×80
PDB id:
6v2s
Name: Gene regulation
Title: Crystal structure of chromodomain of mpp8 in complex with inhibitor unc3866
Structure: M-phase phosphoprotein 8. Chain: a, b. Fragment: chromodomain. Synonym: two hybrid-associated protein 3 with ranbpm,twa3. Engineered: yes. Unc3866. Chain: c, d. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: mphosph8, mpp8. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: -v2r-prare2. Synthetic: yes. Synthetic construct.
Resolution:
1.60Å     R-factor:   0.210     R-free:   0.243
Authors: Y.Liu,W.Tempel,J.R.Walker,C.Bountra,C.H.Arrowsmith,A.M.Edwards,J.Min, Structural Genomics Consortium (Sgc)
Key ref: C.Dong et al. (2020). Structural Basis for the Binding Selectivity of Human CDY Chromodomains. Cell Chem Biol, 27, 827. PubMed id: 32470319 DOI: 10.1016/j.chembiol.2020.05.007
Date:
25-Nov-19     Release date:   25-Dec-19    
PROCHECK
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 Headers
 References

Protein chains
Q99549  (MPP8_HUMAN) -  M-phase phosphoprotein 8 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
860 a.a.
60 a.a.
Key:    Secondary structure

 

 
DOI no: 10.1016/j.chembiol.2020.05.007 Cell Chem Biol 27:827 (2020)
PubMed id: 32470319  
 
 
Structural Basis for the Binding Selectivity of Human CDY Chromodomains.
C.Dong, Y.Liu, T.J.Lyu, S.Beldar, K.N.Lamb, W.Tempel, Y.Li, Z.Li, L.I.James, S.Qin, Y.Wang, J.Min.
 
  ABSTRACT  
 
The CDY (chromodomain on the Y) proteins play an essential role in normal spermatogenesis and brain development. Dysregulation of their expression has been linked to male infertility and various neurological diseases. Like the chromodomains of HP1 and Polycomb, the CDY chromodomains also recognize the lysine-methylated ARKS motif embedded in histone and non-histone proteins. Interestingly, the CDY chromodomains exhibit different binding preferences for the lysine-methylated ARKS motif in different sequence contexts. Here, we present the structural basis for selective binding of CDY1 to H3K9me3 and preferential binding of CDYL2 to H3tK27me3 over H3K27me3. In addition, we use a CDYL1/2-selective compound, UNC4850, to gain further insight into the molecular mechanisms underlying CDYL2 binding specificity. Our work also provides critical implications that CDYL1b's role in the regulation of neural development is dependent on its recognition of the lysine-methylated ARKS motif.
 

 

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