1zs8

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[[Image:1zs8.gif|left|200px]]<br /><applet load="1zs8" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zs8.gif|left|200px]]
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caption="1zs8, resolution 3.00&Aring;" />
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'''Crystal Structure of the Murine MHC Class Ib Molecule M10.5'''<br />
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{{Structure
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|PDB= 1zs8 |SIZE=350|CAPTION= <scene name='initialview01'>1zs8</scene>, resolution 3.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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|ACTIVITY=
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|GENE= M10.5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), B2M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal Structure of the Murine MHC Class Ib Molecule M10.5'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ZS8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZS8 OCA].
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1ZS8 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZS8 OCA].
==Reference==
==Reference==
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Structure of a pheromone receptor-associated MHC molecule with an open and empty groove., Olson R, Huey-Tubman KE, Dulac C, Bjorkman PJ, PLoS Biol. 2005 Aug;3(8):e257. Epub 2005 Jul 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16089503 16089503]
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Structure of a pheromone receptor-associated MHC molecule with an open and empty groove., Olson R, Huey-Tubman KE, Dulac C, Bjorkman PJ, PLoS Biol. 2005 Aug;3(8):e257. Epub 2005 Jul 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16089503 16089503]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: major histocompatibility complex]]
[[Category: major histocompatibility complex]]
[[Category: mhc]]
[[Category: mhc]]
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[[Category: peptides]]
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[[Category: peptide]]
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[[Category: pheromone receptors]]
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[[Category: pheromone receptor]]
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[[Category: v2r receptors]]
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[[Category: v2r receptor]]
[[Category: vno]]
[[Category: vno]]
[[Category: vomeronasal organ]]
[[Category: vomeronasal organ]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:18:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:39:15 2008''

Revision as of 13:39, 20 March 2008


PDB ID 1zs8

Drag the structure with the mouse to rotate
, resolution 3.00Å
Ligands:
Gene: M10.5 (Mus musculus), B2M (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the Murine MHC Class Ib Molecule M10.5


Contents

Overview

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.

Disease

Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]

About this Structure

1ZS8 is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

Reference

Structure of a pheromone receptor-associated MHC molecule with an open and empty groove., Olson R, Huey-Tubman KE, Dulac C, Bjorkman PJ, PLoS Biol. 2005 Aug;3(8):e257. Epub 2005 Jul 12. PMID:16089503

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