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.


1p4l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1p4l.gif|left|200px]]<br /><applet load="1p4l" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1p4l.gif|left|200px]]
-
caption="1p4l, resolution 2.90&Aring;" />
+
 
-
'''Crystal structure of NK receptor Ly49C mutant with its MHC class I ligand H-2Kb'''<br />
+
{{Structure
 +
|PDB= 1p4l |SIZE=350|CAPTION= <scene name='initialview01'>1p4l</scene>, resolution 2.90&Aring;
 +
|SITE=
 +
|LIGAND=
 +
|ACTIVITY=
 +
|GENE= H2-K ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), B2M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), KLRA3 OR LY49C OR LY-49C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
 +
}}
 +
 
 +
'''Crystal structure of NK receptor Ly49C mutant with its MHC class I ligand H-2Kb'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1P4L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P4L OCA].
+
1P4L is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P4L OCA].
==Reference==
==Reference==
-
Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2K(b)., Dam J, Guan R, Natarajan K, Dimasi N, Chlewicki LK, Kranz DM, Schuck P, Margulies DH, Mariuzza RA, Nat Immunol. 2003 Dec;4(12):1213-22. Epub 2003 Nov 2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14595439 14595439]
+
Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2K(b)., Dam J, Guan R, Natarajan K, Dimasi N, Chlewicki LK, Kranz DM, Schuck P, Margulies DH, Mariuzza RA, Nat Immunol. 2003 Dec;4(12):1213-22. Epub 2003 Nov 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14595439 14595439]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 23: Line 32:
[[Category: natural killer receptor]]
[[Category: natural killer receptor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:02 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:19:45 2008''

Revision as of 11:19, 20 March 2008


PDB ID 1p4l

Drag the structure with the mouse to rotate
, resolution 2.90Å
Gene: H2-K (Mus musculus), B2M (Mus musculus), KLRA3 OR LY49C OR LY-49C (Mus musculus)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of NK receptor Ly49C mutant with its MHC class I ligand H-2Kb


Overview

The Ly49 family of natural killer (NK) receptors regulates NK cell function by sensing major histocompatibility complex (MHC) class I. Ly49 receptors show complex patterns of MHC class I cross-reactivity and, in certain cases, peptide selectivity. To investigate whether specificity differences result from topological differences in MHC class I engagement, we determined the structure of the peptide-selective receptor Ly49C in complex with H-2K(b). The Ly49C homodimer binds two MHC class I molecules in symmetrical way, a mode distinct from that of Ly49A, which binds MHC class I asymmetrically. Ly49C does not directly contact the MHC-bound peptide. In addition, MHC crosslinking by Ly49C was demonstrated in solution. We propose a dynamic model for Ly49-MHC class I interactions involving conformational changes in the receptor, whereby variations in Ly49 dimerization mediate different MHC-binding modes.

About this Structure

1P4L is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2K(b)., Dam J, Guan R, Natarajan K, Dimasi N, Chlewicki LK, Kranz DM, Schuck P, Margulies DH, Mariuzza RA, Nat Immunol. 2003 Dec;4(12):1213-22. Epub 2003 Nov 2. PMID:14595439

Page seeded by OCA on Thu Mar 20 13:19:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools