2ask

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|PDB= 2ask |SIZE=350|CAPTION= <scene name='initialview01'>2ask</scene>, resolution 1.55&Aring;
|PDB= 2ask |SIZE=350|CAPTION= <scene name='initialview01'>2ask</scene>, resolution 1.55&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ask FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ask OCA], [http://www.ebi.ac.uk/pdbsum/2ask PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ask RCSB]</span>
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[[Category: Sah, D.]]
[[Category: Sah, D.]]
[[Category: Silvian, L.]]
[[Category: Silvian, L.]]
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[[Category: SO4]]
 
[[Category: glial cell derived family ligand]]
[[Category: glial cell derived family ligand]]
[[Category: neurotrphoic growth factor]]
[[Category: neurotrphoic growth factor]]
[[Category: sulfate]]
[[Category: sulfate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:53:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:56:43 2008''

Revision as of 22:56, 30 March 2008


PDB ID 2ask

Drag the structure with the mouse to rotate
, resolution 1.55Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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