2o27
From Proteopedia
(New page: 200px<br /><applet load="2o27" size="450" color="white" frame="true" align="right" spinBox="true" caption="2o27, resolution 2.20Å" /> '''Structure of a class...) |
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- | [[Image:2o27.gif|left|200px]]<br /><applet load="2o27" size=" | + | [[Image:2o27.gif|left|200px]]<br /><applet load="2o27" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2o27, resolution 2.20Å" /> | caption="2o27, resolution 2.20Å" /> | ||
'''Structure of a class III RTK signaling assembly'''<br /> | '''Structure of a class III RTK signaling assembly'''<br /> | ||
==Overview== | ==Overview== | ||
- | Stem cell factor (SCF) binds to and activates the KIT receptor, a class | + | 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== | ==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:// | + | 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== | ==Reference== | ||
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[[Category: stem cell factor]] | [[Category: stem cell factor]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:13:43 2008'' |
Revision as of 16:13, 21 February 2008
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Structure of a class III RTK signaling assembly
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.
About this Structure
2O27 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis for stem cell factor-KIT signaling and activation of class III receptor tyrosine kinases., Liu H, Chen X, Focia PJ, He X, EMBO J. 2007 Feb 7;26(3):891-901. Epub 2007 Jan 25. PMID:17255936
Page seeded by OCA on Thu Feb 21 18:13:43 2008