1kjm
From Proteopedia
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|PDB= 1kjm |SIZE=350|CAPTION= <scene name='initialview01'>1kjm</scene>, resolution 2.35Å | |PDB= 1kjm |SIZE=350|CAPTION= <scene name='initialview01'>1kjm</scene>, resolution 2.35Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ed3|1ED3]], [[1kjv|1KJV]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kjm OCA], [http://www.ebi.ac.uk/pdbsum/1kjm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kjm RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Trowsdale, J.]] | [[Category: Trowsdale, J.]] | ||
[[Category: Wilson, I A.]] | [[Category: Wilson, I A.]] | ||
| - | [[Category: SO4]] | ||
[[Category: extracellular domain]] | [[Category: extracellular domain]] | ||
[[Category: heterodimer]] | [[Category: heterodimer]] | ||
[[Category: peptide-mhc complex]] | [[Category: peptide-mhc complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:49:32 2008'' |
Revision as of 18:49, 30 March 2008
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| , resolution 2.35Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1ED3, 1KJV
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
TAP-A-associated rat MHC class I molecule
Overview
Antigenic peptides are loaded onto class I MHC molecules in the endoplasmic reticulum (ER) by a complex consisting of the MHC class I heavy chain, beta(2)-microglobulin, calreticulin, tapasin, Erp57 (ER60) and the transporter associated with antigen processing (TAP). While most mammalian species transport these peptides into the ER via a single allele of TAP, rats have evolved different TAPs, TAP-A and TAP-B, that are present in different inbred strains. Each TAP delivers a different spectrum of peptides and is associated genetically with distinct subsets of MHC class Ia alleles, but the molecular basis for the conservation (or co-evolution) of the two transporter alleles is unknown. We have determined the crystal structures of a representative of each MHC subset, viz RT1-A(a) and RT1-A1(c), in association with high-affinity nonamer peptides. The structures reveal how the chemical properties of the two different rat MHC F-pockets match those of the corresponding C termini of the peptides, corroborating biochemical data on the rates of peptide-MHC complex assembly. An unusual sequence in RT1-A1(c) leads to a major deviation from the highly conserved beta(3)/alpha(1) loop (residues 40-59) conformation in mouse and human MHC class I structures. This loop change contributes to profound changes in the shape of the A-pocket in the peptide-binding groove and may explain the function of RT1-A1(c) as an inhibitory natural killer cell ligand.
About this Structure
1KJM is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Crystal structures of two rat MHC class Ia (RT1-A) molecules that are associated differentially with peptide transporter alleles TAP-A and TAP-B., Rudolph MG, Stevens J, Speir JA, Trowsdale J, Butcher GW, Joly E, Wilson IA, J Mol Biol. 2002 Dec 13;324(5):975-90. PMID:12470953
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