2o27

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(New page: 200px<br /><applet load="2o27" size="450" color="white" frame="true" align="right" spinBox="true" caption="2o27, resolution 2.20&Aring;" /> '''Structure of a class...)
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caption="2o27, resolution 2.20&Aring;" />
caption="2o27, resolution 2.20&Aring;" />
'''Structure of a class III RTK signaling assembly'''<br />
'''Structure of a class III RTK signaling assembly'''<br />
==Overview==
==Overview==
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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.
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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==
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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].
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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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:02:00 2007''
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''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


2o27, resolution 2.20Å

Drag the structure with the mouse to rotate

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

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