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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jfm ConSurf]. | ||
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Revision as of 09:13, 9 February 2016
CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETACRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA
Structural highlights
Function[RAE1B_MOUSE] Acts as a ligand for NKG2D.[1] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedInduced by retinoic acid and implicated in playing a role in development, rodent RAE-1 proteins are ligands for the activating immunoreceptor NKG2D, widely expressed on natural killer cells, T cells, and macrophages. RAE-1 proteins (alpha, beta, gamma, and delta) are distant major histocompatibility complex (MHC) class I homologs, comprising isolated alpha1alpha2 platform domains. The crystal structure of RAE-1beta was distorted from other MHC homologs and displayed noncanonical disulfide bonds. The loss of any remnant of a peptide binding groove was facilitated by the close approach of the groove-defining helices through a hydrophobic, leucine-rich interface. The RAE-1beta-murine NKG2D complex structure resembled the human NKG2D-MICA receptor-ligand complex and further demonstrated the promiscuity of the NKG2D ligand binding site. Crystal structures of RAE-1beta and its complex with the activating immunoreceptor NKG2D.,Li P, McDermott G, Strong RK Immunity. 2002 Jan;16(1):77-86. PMID:11825567[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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