spacer
spacer

PDBsum entry 4aen

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Immune system PDB id
4aen
Jmol
Contents
Protein chains
178 a.a.
181 a.a.
15 a.a.
Ligands
GOL ×2
Waters ×249
PDB id:
4aen
Name: Immune system
Title: Hla-dr1 with covalently linked clip106-120 in reversed orien
Structure: Hla class ii histocompatibility antigen, dr alpha chain: a. Fragment: extracellular domain, residues 26-217. Synonym: mhc class ii antigen dra. Engineered: yes. Hla class ii histocompatibility antigen, drb1-1 b chain. Chain: b. Fragment: extracellular domain, residues 30-227.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.20Å     R-factor:   0.185     R-free:   0.220
Authors: A.Schlundt,S.Guenther,J.Sticht,M.Wieczorek,Y.Roske,U.Heinema C.Freund
Key ref: A.Schlundt et al. (2012). Peptide linkage to the α-subunit of MHCII creates a stably inverted antigen presentation complex. J Mol Biol, 423, 294-302. PubMed id: 22820093 DOI: 10.1016/j.jmb.2012.07.008
Date:
11-Jan-12     Release date:   01-Aug-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01903  (DRA_HUMAN) -  HLA class II histocompatibility antigen, DR alpha chain
Seq:
Struc:
254 a.a.
178 a.a.
Protein chain
Pfam   ArchSchema ?
P04229  (2B11_HUMAN) -  HLA class II histocompatibility antigen, DRB1-1 beta chain
Seq:
Struc:
266 a.a.
181 a.a.
Protein chain
Pfam   ArchSchema ?
P04233  (HG2A_HUMAN) -  HLA class II histocompatibility antigen gamma chain
Seq:
Struc:
296 a.a.
15 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   2 terms 
  Biological process     immune response   2 terms 

 

 
DOI no: 10.1016/j.jmb.2012.07.008 J Mol Biol 423:294-302 (2012)
PubMed id: 22820093  
 
 
Peptide linkage to the α-subunit of MHCII creates a stably inverted antigen presentation complex.
A.Schlundt, S.Günther, J.Sticht, M.Wieczorek, Y.Roske, U.Heinemann, C.Freund.
 
  ABSTRACT  
 
No abstract given.