This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1kpr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1kpr.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1kpr.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kpr| PDB=1kpr | SCENE= }}
{{STRUCTURE_1kpr| PDB=1kpr | SCENE= }}
-
'''The human non-classical major histocompatibility complex molecule HLA-E'''
+
===The human non-classical major histocompatibility complex molecule HLA-E===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12411439}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12411439 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12411439}}
==Disease==
==Disease==
Line 32: Line 36:
[[Category: Mhc]]
[[Category: Mhc]]
[[Category: Non-classical mhc]]
[[Category: Non-classical mhc]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:01:24 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:43:53 2008''

Revision as of 07:43, 2 July 2008

Image:1kpr.png

Template:STRUCTURE 1kpr

Contents

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

Template:ABSTRACT PUBMED 12411439

Disease

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

About this Structure

1KPR 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 Wed Jul 2 10:43:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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