2ask

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(New page: 200px<br /> <applet load="2ask" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ask, resolution 1.55&Aring;" /> '''Structure of human ...)
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[[Image:2ask.gif|left|200px]]<br /><applet load="2ask" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2ask" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2ask, resolution 1.55&Aring;" />
caption="2ask, resolution 1.55&Aring;" />
'''Structure of human Artemin'''<br />
'''Structure of human Artemin'''<br />
==Overview==
==Overview==
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Artemin (ART) promotes the growth of developing peripheral neurons by, signaling through a multicomponent receptor complex comprised of a, transmembrane tyrosine kinase receptor (cRET) and a specific, glycosylphosphatidylinositol-linked co-receptor (GFRalpha3). Glial cell, line-derived neurotrophic factor (GDNF) signals through a similar ternary, complex but requires heparan sulfate proteoglycans (HSPGs) for full, activity. HSPG has not been demonstrated as a requirement for ART, signaling. We crystallized ART in the presence of sulfate and solved its, structure by isomorphous replacement. The structure reveals ordered, sulfate anions bound to arginine residues in the pre-helix and, amino-terminal regions that were organized in a triad arrangement, characteristic of heparan sulfate. Three residues in the pre-helix were, singly or triply substituted with glutamic acid, and the resulting, proteins were shown to have reduced heparin-binding affinity that is, partly reflected in their ability to activate cRET. This study suggests, that ART binds HSPGs and identifies residues that may be involved in HSPG, binding.
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Artemin (ART) promotes the growth of developing peripheral neurons by signaling through a multicomponent receptor complex comprised of a transmembrane tyrosine kinase receptor (cRET) and a specific glycosylphosphatidylinositol-linked co-receptor (GFRalpha3). Glial cell line-derived neurotrophic factor (GDNF) signals through a similar ternary complex but requires heparan sulfate proteoglycans (HSPGs) for full activity. HSPG has not been demonstrated as a requirement for ART signaling. We crystallized ART in the presence of sulfate and solved its structure by isomorphous replacement. The structure reveals ordered sulfate anions bound to arginine residues in the pre-helix and amino-terminal regions that were organized in a triad arrangement characteristic of heparan sulfate. Three residues in the pre-helix were singly or triply substituted with glutamic acid, and the resulting proteins were shown to have reduced heparin-binding affinity that is partly reflected in their ability to activate cRET. This study suggests that ART binds HSPGs and identifies residues that may be involved in HSPG binding.
==About this Structure==
==About this Structure==
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2ASK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ASK OCA].
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2ASK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ASK OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Boriack-Sjodin, P.A.]]
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[[Category: Boriack-Sjodin, P A.]]
[[Category: Carmillo, P.]]
[[Category: Carmillo, P.]]
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[[Category: Gong, B.J.]]
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[[Category: Gong, B J.]]
[[Category: Jin, P.]]
[[Category: Jin, P.]]
[[Category: Pelletier, C.]]
[[Category: Pelletier, C.]]
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[[Category: sulfates]]
[[Category: sulfates]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:54:17 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:30:34 2008''

Revision as of 14:30, 21 February 2008


2ask, resolution 1.55Å

Drag the structure with the mouse to rotate

Structure of human Artemin

Overview

Artemin (ART) promotes the growth of developing peripheral neurons by signaling through a multicomponent receptor complex comprised of a transmembrane tyrosine kinase receptor (cRET) and a specific glycosylphosphatidylinositol-linked co-receptor (GFRalpha3). Glial cell line-derived neurotrophic factor (GDNF) signals through a similar ternary complex but requires heparan sulfate proteoglycans (HSPGs) for full activity. HSPG has not been demonstrated as a requirement for ART signaling. We crystallized ART in the presence of sulfate and solved its structure by isomorphous replacement. The structure reveals ordered sulfate anions bound to arginine residues in the pre-helix and amino-terminal regions that were organized in a triad arrangement characteristic of heparan sulfate. Three residues in the pre-helix were singly or triply substituted with glutamic acid, and the resulting proteins were shown to have reduced heparin-binding affinity that is partly reflected in their ability to activate cRET. This study suggests that ART binds HSPGs and identifies residues that may be involved in HSPG binding.

About this Structure

2ASK is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Artemin crystal structure reveals insights into heparan sulfate binding., Silvian L, Jin P, Carmillo P, Boriack-Sjodin PA, Pelletier C, Rushe M, Gong B, Sah D, Pepinsky B, Rossomando A, Biochemistry. 2006 Jun 6;45(22):6801-12. PMID:16734417

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