1p1z

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1p1z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p1z, resolution 3.26&Aring;" /> '''X-RAY CRYSTAL STRUCT...)
Line 1: Line 1:
-
[[Image:1p1z.gif|left|200px]]<br /><applet load="1p1z" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1p1z.gif|left|200px]]<br /><applet load="1p1z" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1p1z, resolution 3.26&Aring;" />
caption="1p1z, resolution 3.26&Aring;" />
'''X-RAY CRYSTAL STRUCTURE OF THE LECTIN-LIKE NATURAL KILLER CELL RECEPTOR LY-49C BOUND TO ITS MHC CLASS I LIGAND H-2Kb'''<br />
'''X-RAY CRYSTAL STRUCTURE OF THE LECTIN-LIKE NATURAL KILLER CELL RECEPTOR LY-49C BOUND TO ITS MHC CLASS I LIGAND H-2Kb'''<br />
==Overview==
==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.
+
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==
==About this Structure==
-
1P1Z 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P1Z OCA].
+
1P1Z 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=1P1Z OCA].
==Reference==
==Reference==
Line 15: Line 15:
[[Category: Dam, J.]]
[[Category: Dam, J.]]
[[Category: Dimasi, N.]]
[[Category: Dimasi, N.]]
-
[[Category: Margulies, D.H.]]
+
[[Category: Margulies, D H.]]
-
[[Category: Mariuzza, R.A.]]
+
[[Category: Mariuzza, R A.]]
[[Category: Natarajan, K.]]
[[Category: Natarajan, K.]]
[[Category: Rangjin, G.]]
[[Category: Rangjin, G.]]
Line 26: Line 26:
[[Category: ova]]
[[Category: ova]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:23:56 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:24:14 2008''

Revision as of 12:24, 21 February 2008

Image:1p1z.gif

1p1z, resolution 3.26Å

Drag the structure with the mouse to rotate

X-RAY CRYSTAL STRUCTURE OF THE LECTIN-LIKE NATURAL KILLER CELL RECEPTOR LY-49C BOUND TO 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

1P1Z 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 Feb 21 14:24:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p1z"
Personal tools