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PDBsum entry 4jqw

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protein ligands Protein-protein interface(s) links
Apoptosis/signalling protein PDB id
4jqw

 

 

 

 

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Contents
Protein chains
92 a.a.
73 a.a.
Ligands
PO4
PDB id:
4jqw
Name: Apoptosis/signalling protein
Title: Crystal structure of a complex of nod1 card and ubiquitin
Structure: Nucleotide-binding oligomerization domain-containing protein 1. Chain: a. Fragment: card domain. Synonym: caspase recruitment domain-containing protein 4. Engineered: yes. Polyubiquitin-c. Chain: c. Fragment: ubiquitin.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: card4, nod1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: ubc.
Resolution:
2.90Å     R-factor:   0.230     R-free:   0.270
Authors: A.M.Ver Heul,L.Gakhar,R.C.Piper,S.Ramaswamy
Key ref: A.M.Ver Heul et al. (2014). Crystal structure of a complex of NOD1 CARD and ubiquitin. Plos One, 9, e104017. PubMed id: 25127239 DOI: 10.1371/journal.pone.0104017
Date:
20-Mar-13     Release date:   26-Mar-14    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9Y239  (NOD1_HUMAN) -  Nucleotide-binding oligomerization domain-containing protein 1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
953 a.a.
92 a.a.*
Protein chain
Pfam   ArchSchema ?
P0CG48  (UBC_HUMAN) -  Polyubiquitin-C from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
685 a.a.
73 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
DOI no: 10.1371/journal.pone.0104017 Plos One 9:e104017 (2014)
PubMed id: 25127239  
 
 
Crystal structure of a complex of NOD1 CARD and ubiquitin.
A.M.Ver Heul, L.Gakhar, R.C.Piper, R.Subramanian.
 
  ABSTRACT  
 
The Caspase Recruitment Domain (CARD) from the innate immune receptor NOD1 was crystallized with Ubiquitin (Ub). NOD1 CARD was present as a helix-swapped homodimer similar to other structures of NOD1 CARD, and Ub monomers formed a homodimer similar in conformation to Lys48-linked di-Ub. The interaction between NOD1 CARD and Ub in the crystal was mediated by novel binding sites on each molecule. Comparisons of these sites to previously identified interaction surfaces on both molecules were made along with discussion of their potential functional significance.
 

 

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