1jgd
From Proteopedia
(New page: 200px<br /> <applet load="1jgd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jgd, resolution 1.9Å" /> '''HLA-B*2709 bound to ...) |
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| - | [[Image:1jgd.gif|left|200px]]<br /> | + | [[Image:1jgd.gif|left|200px]]<br /><applet load="1jgd" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1jgd" size=" | + | |
caption="1jgd, resolution 1.9Å" /> | caption="1jgd, resolution 1.9Å" /> | ||
'''HLA-B*2709 bound to deca-peptide s10R'''<br /> | '''HLA-B*2709 bound to deca-peptide s10R'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Selected HLA-B27 subtypes are associated with spondyloarthropathies, but | + | Selected HLA-B27 subtypes are associated with spondyloarthropathies, but the underlying mechanism is not understood. To explain this association in molecular terms, a comparison of peptide-dependent dynamic and structural properties of the differentially disease-associated subtypes HLA-B*2705 and HLA-B*2709 was carried out. These molecules differ only by a single amino acid at the floor of the peptide binding groove. The thermostabilities of a series of HLA-B27 molecules complexed with nonameric and decameric peptides were determined and revealed substantial differences depending on the subtype as well as the residues at the termini of the peptides. In addition we present the crystal structure of the B*2709 subtype complexed with a decameric peptide. This structure provides an explanation for the preference of HLA-B27 for a peptide with an N-terminal arginine as secondary anchor and the lack of preference for tyrosine as peptide C terminus in B*2709. The data show that differences in thermodynamic properties between peptide-complexed HLA-B27 subtypes are correlated with a variety of structural properties. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JGD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1JGD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JGD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Hillig, R | + | [[Category: Hillig, R C.]] |
[[Category: Huelsmeyer, M.]] | [[Category: Huelsmeyer, M.]] | ||
[[Category: Saenger, W.]] | [[Category: Saenger, W.]] | ||
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[[Category: mhc (major histocompatibility complex)]] | [[Category: mhc (major histocompatibility complex)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:22:21 2008'' |
Revision as of 11:22, 21 February 2008
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HLA-B*2709 bound to deca-peptide s10R
Contents |
Overview
Selected HLA-B27 subtypes are associated with spondyloarthropathies, but the underlying mechanism is not understood. To explain this association in molecular terms, a comparison of peptide-dependent dynamic and structural properties of the differentially disease-associated subtypes HLA-B*2705 and HLA-B*2709 was carried out. These molecules differ only by a single amino acid at the floor of the peptide binding groove. The thermostabilities of a series of HLA-B27 molecules complexed with nonameric and decameric peptides were determined and revealed substantial differences depending on the subtype as well as the residues at the termini of the peptides. In addition we present the crystal structure of the B*2709 subtype complexed with a decameric peptide. This structure provides an explanation for the preference of HLA-B27 for a peptide with an N-terminal arginine as secondary anchor and the lack of preference for tyrosine as peptide C terminus in B*2709. The data show that differences in thermodynamic properties between peptide-complexed HLA-B27 subtypes are correlated with a variety of structural properties.
Disease
Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142830], Hypoproteinemia, hypercatabolic OMIM:[109700], Spondyloarthropathy, susceptibility to, 1 OMIM:[142830], Stevens-Johnson syndrome, carbamazepine-induced, susceptibility to OMIM:[142830]
About this Structure
1JGD is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Thermodynamic and structural analysis of peptide- and allele-dependent properties of two HLA-B27 subtypes exhibiting differential disease association., Hillig RC, Hulsmeyer M, Saenger W, Welfle K, Misselwitz R, Welfle H, Kozerski C, Volz A, Uchanska-Ziegler B, Ziegler A, J Biol Chem. 2004 Jan 2;279(1):652-63. Epub 2003 Oct 10. PMID:14555655
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