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1jsk

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(New page: 200px<br /><applet load="1jsk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jsk, resolution 3.50&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1jsk.gif|left|200px]]<br /><applet load="1jsk" size="350" color="white" frame="true" align="right" spinBox="true"
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'''CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA IN COMPLEX WITH NKG2D'''<br />
'''CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA IN COMPLEX WITH NKG2D'''<br />
==Overview==
==Overview==
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Induced by retinoic acid and implicated in playing a role in development, rodent RAE-1 proteins are ligands for the activating immunoreceptor NKG2D, widely expressed on natural killer cells, T cells, and macrophages. RAE-1, proteins (alpha, beta, gamma, and delta) are distant major, histocompatibility complex (MHC) class I homologs, comprising isolated, alpha1alpha2 platform domains. The crystal structure of RAE-1beta was, distorted from other MHC homologs and displayed noncanonical disulfide, bonds. The loss of any remnant of a peptide binding groove was facilitated, by the close approach of the groove-defining helices through a, hydrophobic, leucine-rich interface. The RAE-1beta-murine NKG2D complex, structure resembled the human NKG2D-MICA receptor-ligand complex and, further demonstrated the promiscuity of the NKG2D ligand binding site.
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Induced by retinoic acid and implicated in playing a role in development, rodent RAE-1 proteins are ligands for the activating immunoreceptor NKG2D, widely expressed on natural killer cells, T cells, and macrophages. RAE-1 proteins (alpha, beta, gamma, and delta) are distant major histocompatibility complex (MHC) class I homologs, comprising isolated alpha1alpha2 platform domains. The crystal structure of RAE-1beta was distorted from other MHC homologs and displayed noncanonical disulfide bonds. The loss of any remnant of a peptide binding groove was facilitated by the close approach of the groove-defining helices through a hydrophobic, leucine-rich interface. The RAE-1beta-murine NKG2D complex structure resembled the human NKG2D-MICA receptor-ligand complex and further demonstrated the promiscuity of the NKG2D ligand binding site.
==About this Structure==
==About this Structure==
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1JSK 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=1JSK OCA].
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1JSK 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=1JSK OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Li, P.]]
[[Category: Li, P.]]
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[[Category: Strong, R.K.]]
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[[Category: Strong, R K.]]
[[Category: immune system]]
[[Category: immune system]]
[[Category: mhc-i platform]]
[[Category: mhc-i platform]]
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[[Category: rae-1 beta]]
[[Category: rae-1 beta]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:32:41 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:14 2008''

Revision as of 11:26, 21 February 2008

Image:1jsk.gif

1jsk, resolution 3.50Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA IN COMPLEX WITH NKG2D

Overview

Induced by retinoic acid and implicated in playing a role in development, rodent RAE-1 proteins are ligands for the activating immunoreceptor NKG2D, widely expressed on natural killer cells, T cells, and macrophages. RAE-1 proteins (alpha, beta, gamma, and delta) are distant major histocompatibility complex (MHC) class I homologs, comprising isolated alpha1alpha2 platform domains. The crystal structure of RAE-1beta was distorted from other MHC homologs and displayed noncanonical disulfide bonds. The loss of any remnant of a peptide binding groove was facilitated by the close approach of the groove-defining helices through a hydrophobic, leucine-rich interface. The RAE-1beta-murine NKG2D complex structure resembled the human NKG2D-MICA receptor-ligand complex and further demonstrated the promiscuity of the NKG2D ligand binding site.

About this Structure

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

Reference

Crystal structures of RAE-1beta and its complex with the activating immunoreceptor NKG2D., Li P, McDermott G, Strong RK, Immunity. 2002 Jan;16(1):77-86. PMID:11825567

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