1hkf: Difference between revisions

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[[Image:1hkf.gif|left|200px]]<br />

[[Image:1hkf.gif|left|200px]]<br /><applet load="1hkf" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1hkf" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1hkf, resolution 2.2Å" />

'''THE THREE DIMENSIONAL STRUCTURE OF NK CELL RECEPTOR NKP44, A TRIGGERING PARTNER IN NATURAL CYTOTOXICITY'''<br />

==Overview==

Natural killer (NK) cells direct cytotoxicity against tumor or virally, infected cells. NK cell activation depends on a fine balance between, inhibitory and activating receptors. NKp44 is a cytotoxicity activating, receptor composed of one Ig-like extracellular domain, a transmembrane, segment, and a cytoplasmic domain. The 2.2 A crystal structure shows that, the NKp44 Ig domain forms a saddle-shaped dimer, where a charged surface, groove protrudes from the core structure in each subunit. NKp44 Ig domain, disulfide bridge topology defines a new Ig structural subfamily. The data, presented are a first step toward understanding the molecular basis for, ligand recognition by natural cytotoxicity receptors, whose key role in, the immune system is established, but whose cellular ligands are still, elusive.

Natural killer (NK) cells direct cytotoxicity against tumor or virally infected cells. NK cell activation depends on a fine balance between inhibitory and activating receptors. NKp44 is a cytotoxicity activating receptor composed of one Ig-like extracellular domain, a transmembrane segment, and a cytoplasmic domain. The 2.2 A crystal structure shows that the NKp44 Ig domain forms a saddle-shaped dimer, where a charged surface groove protrudes from the core structure in each subunit. NKp44 Ig domain disulfide bridge topology defines a new Ig structural subfamily. The data presented are a first step toward understanding the molecular basis for ligand recognition by natural cytotoxicity receptors, whose key role in the immune system is established, but whose cellular ligands are still elusive.

==About this Structure==

1HKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1HKF OCA].

1HKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1HKF OCA].

==Reference==

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[[Category: receptor]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 17~~:19:~~20 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:08 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1hkf.gif|left|200px]]<br />
+[[Image:1hkf.gif|left|200px]]<br /><applet load="1hkf" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1hkf" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1hkf, resolution 2.2&Aring;" />
 '''THE THREE DIMENSIONAL STRUCTURE OF NK CELL RECEPTOR NKP44, A TRIGGERING PARTNER IN NATURAL CYTOTOXICITY'''<br />
 ==Overview==
-Natural killer (NK) cells direct cytotoxicity against tumor or virally, infected cells. NK cell activation depends on a fine balance between, inhibitory and activating receptors. NKp44 is a cytotoxicity activating, receptor composed of one Ig-like extracellular domain, a transmembrane, segment, and a cytoplasmic domain. The 2.2 A crystal structure shows that, the NKp44 Ig domain forms a saddle-shaped dimer, where a charged surface, groove protrudes from the core structure in each subunit. NKp44 Ig domain, disulfide bridge topology defines a new Ig structural subfamily. The data, presented are a first step toward understanding the molecular basis for, ligand recognition by natural cytotoxicity receptors, whose key role in, the immune system is established, but whose cellular ligands are still, elusive.
+Natural killer (NK) cells direct cytotoxicity against tumor or virally infected cells. NK cell activation depends on a fine balance between inhibitory and activating receptors. NKp44 is a cytotoxicity activating receptor composed of one Ig-like extracellular domain, a transmembrane segment, and a cytoplasmic domain. The 2.2 A crystal structure shows that the NKp44 Ig domain forms a saddle-shaped dimer, where a charged surface groove protrudes from the core structure in each subunit. NKp44 Ig domain disulfide bridge topology defines a new Ig structural subfamily. The data presented are a first step toward understanding the molecular basis for ligand recognition by natural cytotoxicity receptors, whose key role in the immune system is established, but whose cellular ligands are still elusive.
 ==About this Structure==
-HKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1HKF OCA].
+HKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1HKF OCA].
 ==Reference==
@@ Line 28: / Line 27: @@
 [[Category: receptor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:19:20 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:08 2008''