1xzz

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(New page: 200px<br /><applet load="1xzz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xzz, resolution 1.80&Aring;" /> '''Crystal structure of...)
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[[Image:1xzz.gif|left|200px]]<br /><applet load="1xzz" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1xzz, resolution 1.80&Aring;" />
caption="1xzz, resolution 1.80&Aring;" />
'''Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor'''<br />
'''Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor'''<br />
==Overview==
==Overview==
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Binding of inositol 1,4,5-trisphosphate (IP(3)) to the amino-terminal, region of IP(3) receptor promotes Ca(2+) release from the endoplasmic, reticulum. Within the amino terminus, the first 220 residues directly, preceding the IP(3) binding core domain play a key role in IP(3) binding, suppression and regulatory protein interaction. Here we present a crystal, structure of the suppressor domain of the mouse type 1 IP(3) receptor at, 1.8 A. Displaying a shape akin to a hammer, the suppressor region contains, a Head subdomain forming the beta-trefoil fold and an Arm subdomain, possessing a helix-turn-helix structure. The conserved region on the Head, subdomain appeared to interact with the IP(3) binding core domain and is, in close proximity to the previously proposed binding sites of Homer, RACK1, calmodulin, and CaBP1. The present study sheds light onto the, mechanism underlying the receptor's sensitivity to the ligand and its, communication with cellular signaling proteins.
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Binding of inositol 1,4,5-trisphosphate (IP(3)) to the amino-terminal region of IP(3) receptor promotes Ca(2+) release from the endoplasmic reticulum. Within the amino terminus, the first 220 residues directly preceding the IP(3) binding core domain play a key role in IP(3) binding suppression and regulatory protein interaction. Here we present a crystal structure of the suppressor domain of the mouse type 1 IP(3) receptor at 1.8 A. Displaying a shape akin to a hammer, the suppressor region contains a Head subdomain forming the beta-trefoil fold and an Arm subdomain possessing a helix-turn-helix structure. The conserved region on the Head subdomain appeared to interact with the IP(3) binding core domain and is in close proximity to the previously proposed binding sites of Homer, RACK1, calmodulin, and CaBP1. The present study sheds light onto the mechanism underlying the receptor's sensitivity to the ligand and its communication with cellular signaling proteins.
==About this Structure==
==About this Structure==
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1XZZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XZZ OCA].
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1XZZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XZZ OCA].
==Reference==
==Reference==
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[[Category: ip3 receptor suppressor domain]]
[[Category: ip3 receptor suppressor domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:27:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:00:24 2008''

Revision as of 14:00, 21 February 2008


1xzz, resolution 1.80Å

Drag the structure with the mouse to rotate

Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor

Overview

Binding of inositol 1,4,5-trisphosphate (IP(3)) to the amino-terminal region of IP(3) receptor promotes Ca(2+) release from the endoplasmic reticulum. Within the amino terminus, the first 220 residues directly preceding the IP(3) binding core domain play a key role in IP(3) binding suppression and regulatory protein interaction. Here we present a crystal structure of the suppressor domain of the mouse type 1 IP(3) receptor at 1.8 A. Displaying a shape akin to a hammer, the suppressor region contains a Head subdomain forming the beta-trefoil fold and an Arm subdomain possessing a helix-turn-helix structure. The conserved region on the Head subdomain appeared to interact with the IP(3) binding core domain and is in close proximity to the previously proposed binding sites of Homer, RACK1, calmodulin, and CaBP1. The present study sheds light onto the mechanism underlying the receptor's sensitivity to the ligand and its communication with cellular signaling proteins.

About this Structure

1XZZ is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor., Bosanac I, Yamazaki H, Matsu-Ura T, Michikawa T, Mikoshiba K, Ikura M, Mol Cell. 2005 Jan 21;17(2):193-203. PMID:15664189

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