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PDBsum entry 1zs8
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Immune system
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PDB id
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1zs8
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References listed in PDB file
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Key reference
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Title
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Structure of a pheromone receptor-Associated mhc molecule with an open and empty groove.
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Authors
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R.Olson,
K.E.Huey-Tubman,
C.Dulac,
P.J.Bjorkman.
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Ref.
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Plos Biol, 2005,
3,
e257.
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PubMed id
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Abstract
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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.
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