1ktl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ktl.gif|left|200px]]<br /><applet load="1ktl" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ktl.gif|left|200px]]
-
caption="1ktl, resolution 3.10&Aring;" />
+
 
-
'''The human non-classical major histocompatibility complex molecule HLA-E'''<br />
+
{{Structure
 +
|PDB= 1ktl |SIZE=350|CAPTION= <scene name='initialview01'>1ktl</scene>, resolution 3.10&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
 +
|ACTIVITY=
 +
|GENE= HLA-E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), B2M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
 +
}}
 +
 
 +
'''The human non-classical major histocompatibility complex molecule HLA-E'''
 +
 
==Overview==
==Overview==
Line 10: Line 19:
==About this Structure==
==About this Structure==
-
1KTL 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KTL OCA].
+
1KTL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KTL OCA].
==Reference==
==Reference==
-
HLA-E allelic variants. Correlating differential expression, peptide affinities, crystal structures, and thermal stabilities., Strong RK, Holmes MA, Li P, Braun L, Lee N, Geraghty DE, J Biol Chem. 2003 Feb 14;278(7):5082-90. Epub 2002 Oct 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12411439 12411439]
+
HLA-E allelic variants. Correlating differential expression, peptide affinities, crystal structures, and thermal stabilities., Strong RK, Holmes MA, Li P, Braun L, Lee N, Geraghty DE, J Biol Chem. 2003 Feb 14;278(7):5082-90. Epub 2002 Oct 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12411439 12411439]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 25: Line 34:
[[Category: non-classical mhc]]
[[Category: non-classical mhc]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:46 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:21:59 2008''

Revision as of 10:22, 20 March 2008

Image:1ktl.gif


PDB ID 1ktl

Drag the structure with the mouse to rotate
, resolution 3.10Å
Ligands:
Gene: HLA-E (Homo sapiens), B2M (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



The human non-classical major histocompatibility complex molecule HLA-E


Contents

Overview

Previous studies of HLA-E allelic polymorphism have indicated that balancing selection may be acting to maintain two major alleles in most populations, indicating that a functional difference may exist between the alleles. The alleles differ at only one amino acid position, where an arginine at position 107 in HLA-E*0101 (E(R)) is replaced by a glycine in HLA-E*0103 (E(G)). To investigate possible functional differences, we have undertaken a study of the physical and biochemical properties of these two proteins. By comparing expression levels, we found that whereas steady-state protein levels were similar, the two alleles did in fact differ with respect to cell surface levels. To help explain this difference, we undertook studies of the relative differences in peptide affinity, complex stability, and three-dimensional structure between the alleles. The crystal structures for HLA-E(G) complexed with two distinct peptides were determined, and both were compared with the HLA-E(R) structure. No significant differences in the structure of HLA-E were induced as a result of binding different peptides or by the allelic substitution at position 107. However, there were clear differences in the relative affinity for peptide of each heavy chain, which correlated with and may be explained by differences between their thermal stabilities. These differences were completely consistent with the relative levels of the HLA-E alleles on the cell surface and may indeed correlate with functional differences. This in turn may help explain the apparent balancing selection acting on this locus.

Disease

Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]

About this Structure

1KTL is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

HLA-E allelic variants. Correlating differential expression, peptide affinities, crystal structures, and thermal stabilities., Strong RK, Holmes MA, Li P, Braun L, Lee N, Geraghty DE, J Biol Chem. 2003 Feb 14;278(7):5082-90. Epub 2002 Oct 30. PMID:12411439

Page seeded by OCA on Thu Mar 20 12:21:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ktl"
Personal tools