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PDBsum entry 1zs8
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protein ligands Protein-protein interface(s) links
Immune system PDB id
1zs8

 

 

 

 

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Contents
Protein chains
261 a.a. *
99 a.a. *
Ligands
NAG ×5
* Residue conservation analysis
PDB id:
1zs8
Name: Immune system
Title: Crystal structure of the murine mhc class ib molecule m10.5
Structure: Histocompatibility 2, m region locus 10.5. Chain: a, c, e, g, i. Engineered: yes. Beta-2-microglobulin. Chain: b, d, f, h, j. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: m10.5. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Homo sapiens. Human. Organism_taxid: 9606.
Biol. unit: Dimer (from PQS)
Resolution:
3.00Å     R-factor:   0.307     R-free:   0.308
Authors: R.Olson,K.E.Huey-Tubman,C.Dulac,P.J.Bjorkman
Key ref: R.Olson et al. (2005). Structure of a pheromone receptor-associated MHC molecule with an open and empty groove. Plos Biol, 3, e257. PubMed id: 16089503
Date:
22-Jul-05     Release date:   26-Jul-05    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q860W6  (Q860W6_MOUSE) -  Major histocompatibility complex class Ib M10.5 (Fragment) from Mus musculus
Seq:
Struc: 		327 a.a.
261 a.a.
Protein chains
Pfam   ArchSchema ?
P61769  (B2MG_HUMAN) -  Beta-2-microglobulin from Homo sapiens
Seq:
Struc: 		119 a.a.
99 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Plos Biol 3:e257 (2005)
PubMed id: 16089503  
 
 
Structure of a pheromone receptor-associated MHC molecule with an open and empty groove.
R.Olson, K.E.Huey-Tubman, C.Dulac, P.J.Bjorkman.
 
  ABSTRACT  
 
Neurons in the murine vomeronasal organ (VNO) express a family of class Ib major histocompatibility complex (MHC) proteins (M10s) that interact with the V2R class of VNO receptors. This interaction may play a direct role in the detection of pheromonal cues that initiate reproductive and territorial behaviors. The crystal structure of M10.5, an M10 family member, is similar to that of classical MHC molecules. However, the M10.5 counterpart of the MHC peptide-binding groove is open and unoccupied, revealing the first structure of an empty class I MHC molecule. Similar to empty MHC molecules, but unlike peptide-filled MHC proteins and non-peptide-binding MHC homologs, M10.5 is thermally unstable, suggesting that its groove is normally occupied. However, M10.5 does not bind endogenous peptides when expressed in mammalian cells or when offered a mixture of class I-binding peptides. The F pocket side of the M10.5 groove is open, suggesting that ligands larger than 8-10-mer class I-binding peptides could fit by extending out of the groove. Moreover, variable residues point up from the groove helices, rather than toward the groove as in classical MHC structures. These data suggest that M10s are unlikely to provide specific recognition of class I MHC-binding peptides, but are consistent with binding to other ligands, including proteins such as the V2Rs.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21050182 A.Van Hateren, E.James, A.Bailey, A.Phillips, N.Dalchau, and T.Elliott (2010).
The cell biology of major histocompatibility complex class I assembly: towards a molecular understanding.
  Tissue Antigens, 76, 259-275.  
20492691 T.G.Mast, J.H.Brann, and D.A.Fadool (2010).
The TRPC2 channel forms protein-protein interactions with Homer and RTP in the rat vomeronasal organ.
  BMC Neurosci, 11, 61.  
19426129 C.Schölz, and R.Tampé (2009).
The peptide-loading complex--antigen translocation and MHC class I loading.
  Biol Chem, 390, 783-794.  
19495996 D.W.Hollar (2009).
Risk for intentional violent death associated with HLA genotypes: a preliminary survey of deceased American organ donors.
  Genetica, 137, 253-264.  
19845639 L.P.Villarreal (2009).
The source of self: genetic parasites and the origin of adaptive immunity.
  Ann N Y Acad Sci, 1178, 194-232.  
18808328 S.D.Munger, T.Leinders-Zufall, and F.Zufall (2009).
Subsystem organization of the mammalian sense of smell.
  Annu Rev Physiol, 71, 115-140.  
19838188 Z.Yang, A.P.West, and P.J.Bjorkman (2009).
Crystal structure of TNFalpha complexed with a poxvirus MHC-related TNF binding protein.
  Nat Struct Mol Biol, 16, 1189-1191.
PDB code: 3it8
17521918 C.Mazza, and B.Malissen (2007).
What guides MHC-restricted TCR recognition?
  Semin Immunol, 19, 225-235.  
17261379 F.A.Arosa, S.G.Santos, and S.J.Powis (2007).
Open conformers: the hidden face of MHC-I molecules.
  Trends Immunol, 28, 115-123.  
17709238 F.Zufall, and T.Leinders-Zufall (2007).
Mammalian pheromone sensing.
  Curr Opin Neurobiol, 17, 483-489.  
16953793 C.Dulac, and S.Wagner (2006).
Genetic analysis of brain circuits underlying pheromone signaling.
  Annu Rev Genet, 40, 449-467.  
17108955 P.A.Brennan, and F.Zufall (2006).
Pheromonal communication in vertebrates.
  Nature, 444, 308-315.  
16698261 R.Olson, C.Dulac, and P.J.Bjorkman (2006).
MHC homologs in the nervous system--they haven't lost their groove.
  Curr Opin Neurobiol, 16, 351-357.  
17116884 S.M.Rizvi, and M.Raghavan (2006).
Direct peptide-regulatable interactions between MHC class I molecules and tapasin.
  Proc Natl Acad Sci U S A, 103, 18220-18225.  
16337283 T.Boehm, and F.Zufall (2006).
MHC peptides and the sensory evaluation of genotype.
  Trends Neurosci, 29, 100-107.  
16365312 J.J.Credle, J.S.Finer-Moore, F.R.Papa, R.M.Stroud, and P.Walter (2005).
On the mechanism of sensing unfolded protein in the endoplasmic reticulum.
  Proc Natl Acad Sci U S A, 102, 18773-18784.
PDB code: 2be1
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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