1fzo
From Proteopedia
(New page: 200px<br /><applet load="1fzo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fzo, resolution 1.80Å" /> '''MHC CLASS I NATURAL ...) |
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| - | [[Image:1fzo.gif|left|200px]]<br /><applet load="1fzo" size=" | + | [[Image:1fzo.gif|left|200px]]<br /><applet load="1fzo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fzo, resolution 1.80Å" /> | caption="1fzo, resolution 1.80Å" /> | ||
'''MHC CLASS I NATURAL MUTANT H-2KBM8 HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND SENDAI VIRUS NUCLEOPROTEIN'''<br /> | '''MHC CLASS I NATURAL MUTANT H-2KBM8 HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND SENDAI VIRUS NUCLEOPROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The K(bm1) and K(bm8) natural mutants of the murine MHC class I molecule | + | The K(bm1) and K(bm8) natural mutants of the murine MHC class I molecule H-2K(b) were originally identified by allograft rejection. They also bind viral peptides VSV8 and SEV9 with high affinity, but their peptide complexes have substantially decreased thermostability, and the K(bm1) complexes do not elicit alloreactive T cell responses. Crystal structures of the four mutant complexes at 1.7-1.9 A resolution are similar to the corresponding wild-type K(b) structures, except in the vicinity of the mutated residues, which alter the electrostatic potential, topology, hydrogen bonding, and local water structure of the peptide binding groove. Thus, these natural K(b) mutations define the minimal perturbations in the peptide environment that alter antigen presentation to T cells and abolish alloreactivity. |
==About this Structure== | ==About this Structure== | ||
| - | 1FZO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG, PO4, MRD and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1FZO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=MRD:'>MRD</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FZO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Brunmark, A.]] | [[Category: Brunmark, A.]] | ||
| - | [[Category: Jackson, M | + | [[Category: Jackson, M R.]] |
[[Category: Mattsson, N.]] | [[Category: Mattsson, N.]] | ||
| - | [[Category: Peterson, P | + | [[Category: Peterson, P A.]] |
| - | [[Category: Rudolph, M | + | [[Category: Rudolph, M G.]] |
| - | [[Category: Speir, J | + | [[Category: Speir, J A.]] |
[[Category: Teyton, L.]] | [[Category: Teyton, L.]] | ||
| - | [[Category: Wilson, I | + | [[Category: Wilson, I A.]] |
[[Category: MPD]] | [[Category: MPD]] | ||
[[Category: MRD]] | [[Category: MRD]] | ||
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[[Category: major histocompatibility complex peptide-mhc]] | [[Category: major histocompatibility complex peptide-mhc]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:44:22 2008'' |
Revision as of 10:44, 21 February 2008
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MHC CLASS I NATURAL MUTANT H-2KBM8 HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND SENDAI VIRUS NUCLEOPROTEIN
Overview
The K(bm1) and K(bm8) natural mutants of the murine MHC class I molecule H-2K(b) were originally identified by allograft rejection. They also bind viral peptides VSV8 and SEV9 with high affinity, but their peptide complexes have substantially decreased thermostability, and the K(bm1) complexes do not elicit alloreactive T cell responses. Crystal structures of the four mutant complexes at 1.7-1.9 A resolution are similar to the corresponding wild-type K(b) structures, except in the vicinity of the mutated residues, which alter the electrostatic potential, topology, hydrogen bonding, and local water structure of the peptide binding groove. Thus, these natural K(b) mutations define the minimal perturbations in the peptide environment that alter antigen presentation to T cells and abolish alloreactivity.
About this Structure
1FZO is a Protein complex structure of sequences from Mus musculus with , , and as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structures of K(bm1) and K(bm8) reveal that subtle changes in the peptide environment impact thermostability and alloreactivity., Rudolph MG, Speir JA, Brunmark A, Mattsson N, Jackson MR, Peterson PA, Teyton L, Wilson IA, Immunity. 2001 Mar;14(3):231-42. PMID:11290333
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