2gyr

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(New page: 200px<br /> <applet load="2gyr" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gyr, resolution 2.6&Aring;" /> '''Crystal structure of...)
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caption="2gyr, resolution 2.6&Aring;" />
'''Crystal structure of human artemin'''<br />
'''Crystal structure of human artemin'''<br />
==Overview==
==Overview==
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Artemin (ARTN) is a member of the glial cell line-derived neurotrophic, factor (GDNF) family ligands (GFLs) which regulate the development and, maintenance of many neuronal populations in the mammalian nervous system., Here we report the 1.92 A crystal structure of the complex formed between, ARTN and its receptor GFRalpha3, which is the initiating step in the, formation of a ternary signaling complex containing the shared RET, receptor. It represents a new receptor-ligand interaction mode for the, TGF-beta superfamily that reveals both conserved and, specificity-determining anchor points for all GFL-GFRalpha pairs. In, tandem with the complex structure, cellular studies using receptor, chimeras implicate dyad-symmetric composite interfaces for recruitment and, dimerization of RET, leading to intracellular signaling. These studies, should facilitate the functional dissection of the specific versus, pleiotropic roles of this system in neurobiology, as well as its, exploitation for therapeutic applications.
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Artemin (ARTN) is a member of the glial cell line-derived neurotrophic factor (GDNF) family ligands (GFLs) which regulate the development and maintenance of many neuronal populations in the mammalian nervous system. Here we report the 1.92 A crystal structure of the complex formed between ARTN and its receptor GFRalpha3, which is the initiating step in the formation of a ternary signaling complex containing the shared RET receptor. It represents a new receptor-ligand interaction mode for the TGF-beta superfamily that reveals both conserved and specificity-determining anchor points for all GFL-GFRalpha pairs. In tandem with the complex structure, cellular studies using receptor chimeras implicate dyad-symmetric composite interfaces for recruitment and dimerization of RET, leading to intracellular signaling. These studies should facilitate the functional dissection of the specific versus pleiotropic roles of this system in neurobiology, as well as its exploitation for therapeutic applications.
==About this Structure==
==About this Structure==
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2GYR 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=2GYR OCA].
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2GYR 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=2GYR OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Wang, X.Q.]]
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[[Category: Wang, X Q.]]
[[Category: cystein-knot]]
[[Category: cystein-knot]]
[[Category: neurotrophic factor]]
[[Category: neurotrophic factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:23:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:36:24 2008''

Revision as of 15:36, 21 February 2008


2gyr, resolution 2.6Å

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Crystal structure of human artemin

Overview

Artemin (ARTN) is a member of the glial cell line-derived neurotrophic factor (GDNF) family ligands (GFLs) which regulate the development and maintenance of many neuronal populations in the mammalian nervous system. Here we report the 1.92 A crystal structure of the complex formed between ARTN and its receptor GFRalpha3, which is the initiating step in the formation of a ternary signaling complex containing the shared RET receptor. It represents a new receptor-ligand interaction mode for the TGF-beta superfamily that reveals both conserved and specificity-determining anchor points for all GFL-GFRalpha pairs. In tandem with the complex structure, cellular studies using receptor chimeras implicate dyad-symmetric composite interfaces for recruitment and dimerization of RET, leading to intracellular signaling. These studies should facilitate the functional dissection of the specific versus pleiotropic roles of this system in neurobiology, as well as its exploitation for therapeutic applications.

About this Structure

2GYR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of artemin complexed with its receptor GFRalpha3: convergent recognition of glial cell line-derived neurotrophic factors., Wang X, Baloh RH, Milbrandt J, Garcia KC, Structure. 2006 Jun;14(6):1083-92. PMID:16765900

Page seeded by OCA on Thu Feb 21 17:36:24 2008

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