1qqd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1qqd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qqd, resolution 2.70&Aring;" /> '''CRYSTAL STRUCTURE O...)
Line 1: Line 1:
-
[[Image:1qqd.gif|left|200px]]<br />
+
[[Image:1qqd.gif|left|200px]]<br /><applet load="1qqd" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="1qqd" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="1qqd, resolution 2.70&Aring;" />
caption="1qqd, resolution 2.70&Aring;" />
'''CRYSTAL STRUCTURE OF HLA-CW4, A LIGAND FOR THE KIR2D NATURAL KILLER CELL INHIBITORY RECEPTOR'''<br />
'''CRYSTAL STRUCTURE OF HLA-CW4, A LIGAND FOR THE KIR2D NATURAL KILLER CELL INHIBITORY RECEPTOR'''<br />
==Overview==
==Overview==
-
The crystal structure of the human class I major histocompatibility, complex molecule, human histocompatibility leukocyte antigen (HLA)-Cw4, the ligand for a natural killer (NK) cell inhibitory receptor, has been, determined, complexed with a nonameric consensus peptide (QYDDAVYKL)., Relative to HLA-A2, the peptide binding groove is widened around the COOH, terminus of the alpha 1 helix, which contains residues that determine the, specificity of HLA-Cw4 for the inhibitory NK receptor, KIR2D. The, structure reveals an unusual pattern of internal hydrogen bonding among, peptide residues. The peptide is anchored in four specificity pockets in, the cleft and secured by extensive hydrogen bonds between the peptide main, chain and the cleft. The surface of HLA-Cw4 has electrostatic, complementarity to the surface of the NK cell inhibitory receptor KIR2D.
+
The crystal structure of the human class I major histocompatibility complex molecule, human histocompatibility leukocyte antigen (HLA)-Cw4, the ligand for a natural killer (NK) cell inhibitory receptor, has been determined, complexed with a nonameric consensus peptide (QYDDAVYKL). Relative to HLA-A2, the peptide binding groove is widened around the COOH terminus of the alpha 1 helix, which contains residues that determine the specificity of HLA-Cw4 for the inhibitory NK receptor, KIR2D. The structure reveals an unusual pattern of internal hydrogen bonding among peptide residues. The peptide is anchored in four specificity pockets in the cleft and secured by extensive hydrogen bonds between the peptide main chain and the cleft. The surface of HLA-Cw4 has electrostatic complementarity to the surface of the NK cell inhibitory receptor KIR2D.
==Disease==
==Disease==
Line 11: Line 10:
==About this Structure==
==About this Structure==
-
1QQD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QQD OCA].
+
1QQD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QQD OCA].
==Reference==
==Reference==
Line 17: Line 16:
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
-
[[Category: Fan, Q.R.]]
+
[[Category: Fan, Q R.]]
-
[[Category: Wiley, D.C.]]
+
[[Category: Wiley, D C.]]
[[Category: alpha helix]]
[[Category: alpha helix]]
[[Category: beta sheet]]
[[Category: beta sheet]]
[[Category: immunoglobulin (ig)-like domain]]
[[Category: immunoglobulin (ig)-like domain]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:55:29 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:36 2008''

Revision as of 12:42, 21 February 2008


1qqd, resolution 2.70Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF HLA-CW4, A LIGAND FOR THE KIR2D NATURAL KILLER CELL INHIBITORY RECEPTOR

Contents

Overview

The crystal structure of the human class I major histocompatibility complex molecule, human histocompatibility leukocyte antigen (HLA)-Cw4, the ligand for a natural killer (NK) cell inhibitory receptor, has been determined, complexed with a nonameric consensus peptide (QYDDAVYKL). Relative to HLA-A2, the peptide binding groove is widened around the COOH terminus of the alpha 1 helix, which contains residues that determine the specificity of HLA-Cw4 for the inhibitory NK receptor, KIR2D. The structure reveals an unusual pattern of internal hydrogen bonding among peptide residues. The peptide is anchored in four specificity pockets in the cleft and secured by extensive hydrogen bonds between the peptide main chain and the cleft. The surface of HLA-Cw4 has electrostatic complementarity to the surface of the NK cell inhibitory receptor KIR2D.

Disease

Known diseases associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700], Psoriasis, early onset, susceptibility to OMIM:[142840]

About this Structure

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

Reference

Structure of human histocompatibility leukocyte antigen (HLA)-Cw4, a ligand for the KIR2D natural killer cell inhibitory receptor., Fan QR, Wiley DC, J Exp Med. 1999 Jul 5;190(1):113-23. PMID:10429675

Page seeded by OCA on Thu Feb 21 14:42:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools