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.


1efx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1efx.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1efx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1efx| PDB=1efx | SCENE= }}
{{STRUCTURE_1efx| PDB=1efx | SCENE= }}
-
'''STRUCTURE OF A COMPLEX BETWEEN THE HUMAN NATURAL KILLER CELL RECEPTOR KIR2DL2 AND A CLASS I MHC LIGAND HLA-CW3'''
+
===STRUCTURE OF A COMPLEX BETWEEN THE HUMAN NATURAL KILLER CELL RECEPTOR KIR2DL2 AND A CLASS I MHC LIGAND HLA-CW3===
-
==Overview==
+
<!--
-
Target cell lysis is regulated by natural killer (NK) cell receptors that recognize class I MHC molecules. Here we report the crystal structure of the human immunoglobulin-like NK cell receptor KIR2DL2 in complex with its class I ligand HLA-Cw3 and peptide. KIR binds in a nearly orthogonal orientation across the alpha1 and alpha2 helices of Cw3 and directly contacts positions 7 and 8 of the peptide. No significant conformational changes in KIR occur on complex formation. The receptor footprint on HLA overlaps with but is distinct from that of the T-cell receptor. Charge complementarity dominates the KIR/HLA interface and mutations that disrupt interface salt bridges substantially diminish binding. Most contacts in the complex are between KIR and conserved HLA-C residues, but a hydrogen bond between Lys 44 of KIR2DL2 and Asn 80 of Cw3 confers the allotype specificity. KIR contact requires position 8 of the peptide to be a residue smaller than valine. A second KIR/HLA interface produced an ordered receptor-ligand aggregation in the crystal which may resemble receptor clustering during immune synapse formation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10850706}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10850706 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10850706}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Nk cell receptor]]
[[Category: Nk cell receptor]]
[[Category: Receptor/mhc complex]]
[[Category: Receptor/mhc complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:02:56 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:38:01 2008''

Revision as of 21:38, 30 June 2008

Image:1efx.png

Template:STRUCTURE 1efx

STRUCTURE OF A COMPLEX BETWEEN THE HUMAN NATURAL KILLER CELL RECEPTOR KIR2DL2 AND A CLASS I MHC LIGAND HLA-CW3

Template:ABSTRACT PUBMED 10850706

About this Structure

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

Reference

Crystal structure of an NK cell immunoglobulin-like receptor in complex with its class I MHC ligand., Boyington JC, Motyka SA, Schuck P, Brooks AG, Sun PD, Nature. 2000 Jun 1;405(6786):537-43. PMID:10850706

Page seeded by OCA on Tue Jul 1 00:38:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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