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.


1kjm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1kjm.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1kjm.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kjm| PDB=1kjm | SCENE= }}
{{STRUCTURE_1kjm| PDB=1kjm | SCENE= }}
-
'''TAP-A-associated rat MHC class I molecule'''
+
===TAP-A-associated rat MHC class I molecule===
-
==Overview==
+
<!--
-
Antigenic peptides are loaded onto class I MHC molecules in the endoplasmic reticulum (ER) by a complex consisting of the MHC class I heavy chain, beta(2)-microglobulin, calreticulin, tapasin, Erp57 (ER60) and the transporter associated with antigen processing (TAP). While most mammalian species transport these peptides into the ER via a single allele of TAP, rats have evolved different TAPs, TAP-A and TAP-B, that are present in different inbred strains. Each TAP delivers a different spectrum of peptides and is associated genetically with distinct subsets of MHC class Ia alleles, but the molecular basis for the conservation (or co-evolution) of the two transporter alleles is unknown. We have determined the crystal structures of a representative of each MHC subset, viz RT1-A(a) and RT1-A1(c), in association with high-affinity nonamer peptides. The structures reveal how the chemical properties of the two different rat MHC F-pockets match those of the corresponding C termini of the peptides, corroborating biochemical data on the rates of peptide-MHC complex assembly. An unusual sequence in RT1-A1(c) leads to a major deviation from the highly conserved beta(3)/alpha(1) loop (residues 40-59) conformation in mouse and human MHC class I structures. This loop change contributes to profound changes in the shape of the A-pocket in the peptide-binding groove and may explain the function of RT1-A1(c) as an inhibitory natural killer cell ligand.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12470953}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12470953 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12470953}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Heterodimer]]
[[Category: Heterodimer]]
[[Category: Peptide-mhc complex]]
[[Category: Peptide-mhc complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:49:13 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:26:15 2008''

Revision as of 07:26, 2 July 2008

Template:STRUCTURE 1kjm

TAP-A-associated rat MHC class I molecule

Template:ABSTRACT PUBMED 12470953

About this Structure

1KJM is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structures of two rat MHC class Ia (RT1-A) molecules that are associated differentially with peptide transporter alleles TAP-A and TAP-B., Rudolph MG, Stevens J, Speir JA, Trowsdale J, Butcher GW, Joly E, Wilson IA, J Mol Biol. 2002 Dec 13;324(5):975-90. PMID:12470953

Page seeded by OCA on Wed Jul 2 10:26:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools