2o27: Difference between revisions

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[[Image:2o27.gif|left|200px]]<br /><applet load="2o27" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2o27.gif|left|200px]]<br /><applet load="2o27" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2o27, resolution 2.20Å" />

'''Structure of a class III RTK signaling assembly'''<br />

==Overview==

Stem cell factor (SCF) binds to and activates the KIT receptor, a class, III receptor tyrosine kinase (RTK), to stimulate diverse processes, including melanogenesis, gametogenesis and hematopoeisis. Dysregulation of, KIT activation is associated with many cancers. We report a 2.5 A crystal, structure of the functional core of SCF bound to the extracellular, ligand-binding domains of KIT. The structure reveals a 'wrapping', SCF-recognition mode by KIT, in which KIT adopts a bent conformation to, facilitate each of its first three immunoglobulin (Ig)-like domains to, interact with SCF. Three surface epitopes on SCF, an extended loop, the B, and C helices, and the N-terminal segment, contact distinct KIT domains, with two of the epitopes undergoing large conformational changes upon, receptor binding. The SCF/KIT complex reveals a unique RTK dimerization, assembly, and a novel recognition mode between four-helix bundle cytokines, and Ig-family receptors. It serves as a framework for understanding the, activation mechanisms of class III RTKs.

Stem cell factor (SCF) binds to and activates the KIT receptor, a class III receptor tyrosine kinase (RTK), to stimulate diverse processes including melanogenesis, gametogenesis and hematopoeisis. Dysregulation of KIT activation is associated with many cancers. We report a 2.5 A crystal structure of the functional core of SCF bound to the extracellular ligand-binding domains of KIT. The structure reveals a 'wrapping' SCF-recognition mode by KIT, in which KIT adopts a bent conformation to facilitate each of its first three immunoglobulin (Ig)-like domains to interact with SCF. Three surface epitopes on SCF, an extended loop, the B and C helices, and the N-terminal segment, contact distinct KIT domains, with two of the epitopes undergoing large conformational changes upon receptor binding. The SCF/KIT complex reveals a unique RTK dimerization assembly, and a novel recognition mode between four-helix bundle cytokines and Ig-family receptors. It serves as a framework for understanding the activation mechanisms of class III RTKs.

==About this Structure==

2O27 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=2O27 OCA].

2O27 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=2O27 OCA].

==Reference==

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[[Category: stem cell factor]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 13:~~02:00 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:13:43 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2o27.gif|left|200px]]<br /><applet load="2o27" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2o27.gif|left|200px]]<br /><applet load="2o27" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2o27, resolution 2.20&Aring;" />
 '''Structure of a class III RTK signaling assembly'''<br />
 ==Overview==
-Stem cell factor (SCF) binds to and activates the KIT receptor, a class, III receptor tyrosine kinase (RTK), to stimulate diverse processes, including melanogenesis, gametogenesis and hematopoeisis. Dysregulation of, KIT activation is associated with many cancers. We report a 2.5 A crystal, structure of the functional core of SCF bound to the extracellular, ligand-binding domains of KIT. The structure reveals a 'wrapping', SCF-recognition mode by KIT, in which KIT adopts a bent conformation to, facilitate each of its first three immunoglobulin (Ig)-like domains to, interact with SCF. Three surface epitopes on SCF, an extended loop, the B, and C helices, and the N-terminal segment, contact distinct KIT domains, with two of the epitopes undergoing large conformational changes upon, receptor binding. The SCF/KIT complex reveals a unique RTK dimerization, assembly, and a novel recognition mode between four-helix bundle cytokines, and Ig-family receptors. It serves as a framework for understanding the, activation mechanisms of class III RTKs.
+Stem cell factor (SCF) binds to and activates the KIT receptor, a class III receptor tyrosine kinase (RTK), to stimulate diverse processes including melanogenesis, gametogenesis and hematopoeisis. Dysregulation of KIT activation is associated with many cancers. We report a 2.5 A crystal structure of the functional core of SCF bound to the extracellular ligand-binding domains of KIT. The structure reveals a 'wrapping' SCF-recognition mode by KIT, in which KIT adopts a bent conformation to facilitate each of its first three immunoglobulin (Ig)-like domains to interact with SCF. Three surface epitopes on SCF, an extended loop, the B and C helices, and the N-terminal segment, contact distinct KIT domains, with two of the epitopes undergoing large conformational changes upon receptor binding. The SCF/KIT complex reveals a unique RTK dimerization assembly, and a novel recognition mode between four-helix bundle cytokines and Ig-family receptors. It serves as a framework for understanding the activation mechanisms of class III RTKs.
 ==About this Structure==
-O27 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=2O27 OCA].
+O27 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=2O27 OCA].
 ==Reference==
@@ Line 25: / Line 25: @@
 [[Category: stem cell factor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:02:00 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:13:43 2008''