1hsa
From Proteopedia
(New page: 200px<br /> <applet load="1hsa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hsa, resolution 2.1Å" /> '''THE THREE-DIMENSIONA...) |
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| - | [[Image:1hsa.gif|left|200px]]<br /> | + | [[Image:1hsa.gif|left|200px]]<br /><applet load="1hsa" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1hsa, resolution 2.1Å" /> | caption="1hsa, resolution 2.1Å" /> | ||
'''THE THREE-DIMENSIONAL STRUCTURE OF HLA-B27 AT 2.1 ANGSTROMS RESOLUTION SUGGESTS A GENERAL MECHANISM FOR TIGHT PEPTIDE BINDING TO MHC'''<br /> | '''THE THREE-DIMENSIONAL STRUCTURE OF HLA-B27 AT 2.1 ANGSTROMS RESOLUTION SUGGESTS A GENERAL MECHANISM FOR TIGHT PEPTIDE BINDING TO MHC'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cell surface complexes of class I MHC molecules and bound peptide antigens | + | Cell surface complexes of class I MHC molecules and bound peptide antigens serve as specific recognition elements controlling the cytotoxic immune response. The 2.1 A structure of the human class I MHC molecule HLA-B27 provides a detailed composite image of a co-crystallized collection of HLA-B27-bound peptides, indicating that they share a common main-chain structure and length. It also permits direct visualization of the conservation of arginine as an "anchor" side chain at the second peptide position, which is bound in a potentially HLA-B27-specific pocket and may therefore have a role in the association of HLA-B27 with several diseases. Tight peptide binding to class I MHC molecules appears to result from the extensive contacts found at the ends of the cleft between peptide main-chain atoms and conserved MHC side chains, which also involve the peptide in stabilizing the three-dimensional fold of HLA-B27. The concentration of binding interactions at the peptide termini permits extensive sequence (and probably some length) variability in the center of the peptide, where it is exposed for T cell recognition. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HSA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1HSA with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb62_1.html Major Histocompatibility Complex]]. Full crystallographic information is available from [http:// | + | 1HSA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1HSA with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb62_1.html Major Histocompatibility Complex]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HSA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Major Histocompatibility Complex]] | [[Category: Major Histocompatibility Complex]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Gorga, J | + | [[Category: Gorga, J C.]] |
| - | [[Category: Madden, D | + | [[Category: Madden, D R.]] |
| - | [[Category: Strominger, J | + | [[Category: Strominger, J L.]] |
| - | [[Category: Wiley, D | + | [[Category: Wiley, D C.]] |
[[Category: histocompatibility antigen]] | [[Category: histocompatibility antigen]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:22 2008'' |
Revision as of 11:04, 21 February 2008
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THE THREE-DIMENSIONAL STRUCTURE OF HLA-B27 AT 2.1 ANGSTROMS RESOLUTION SUGGESTS A GENERAL MECHANISM FOR TIGHT PEPTIDE BINDING TO MHC
Contents |
Overview
Cell surface complexes of class I MHC molecules and bound peptide antigens serve as specific recognition elements controlling the cytotoxic immune response. The 2.1 A structure of the human class I MHC molecule HLA-B27 provides a detailed composite image of a co-crystallized collection of HLA-B27-bound peptides, indicating that they share a common main-chain structure and length. It also permits direct visualization of the conservation of arginine as an "anchor" side chain at the second peptide position, which is bound in a potentially HLA-B27-specific pocket and may therefore have a role in the association of HLA-B27 with several diseases. Tight peptide binding to class I MHC molecules appears to result from the extensive contacts found at the ends of the cleft between peptide main-chain atoms and conserved MHC side chains, which also involve the peptide in stabilizing the three-dimensional fold of HLA-B27. The concentration of binding interactions at the peptide termini permits extensive sequence (and probably some length) variability in the center of the peptide, where it is exposed for T cell recognition.
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
1HSA is a Protein complex structure of sequences from Homo sapiens. The following page contains interesting information on the relation of 1HSA with [Major Histocompatibility Complex]. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of HLA-B27 at 2.1 A resolution suggests a general mechanism for tight peptide binding to MHC., Madden DR, Gorga JC, Strominger JL, Wiley DC, Cell. 1992 Sep 18;70(6):1035-48. PMID:1525820
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