2i4k

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(New page: 200px<br /> <applet load="2i4k" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i4k" /> '''Solution Structure of the PX domain of Sort...)
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<applet load="2i4k" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Solution Structure of the PX domain of Sorting Nexin 1'''<br />
'''Solution Structure of the PX domain of Sorting Nexin 1'''<br />
==Overview==
==Overview==
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The sorting nexin (SNX) family of proteins is characterized by, sequence-related phox homology (PX) domains. A minority of PX domains bind, with high affinity to phosphatidylinositol 3-phosphate [PI(3)P], whereas, the majority of PX domains exhibit low affinity that is insufficient to, target them to vesicles. SNX1 is located on endosomes, but its low, affinity PX domain fails to localize in vivo. The NMR structure of the PX, domain of SNX1 reveals an overall fold that is similar to high-affinity PX, domains. However, the phosphatidylinositol (PI) binding pocket of the SNX1, PX domain is incomplete; regions of the pocket that are well defined in, high-affinity PX domains are highly mobile in SNX1. Some of this mobility, is lost upon binding PI(3)P. The C-terminal domain of SNX1 is a long, helical dimer that localizes to vesicles but not to the early endosome, antigen-1-containing vesicles where endogenous SNX1 resides. Thus, the, obligate dimerization of SNX1 that is driven by the C-terminal domain, creates a high-affinity PI binding species that properly targets the holo, protein to endosomes.
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The sorting nexin (SNX) family of proteins is characterized by sequence-related phox homology (PX) domains. A minority of PX domains bind with high affinity to phosphatidylinositol 3-phosphate [PI(3)P], whereas the majority of PX domains exhibit low affinity that is insufficient to target them to vesicles. SNX1 is located on endosomes, but its low affinity PX domain fails to localize in vivo. The NMR structure of the PX domain of SNX1 reveals an overall fold that is similar to high-affinity PX domains. However, the phosphatidylinositol (PI) binding pocket of the SNX1 PX domain is incomplete; regions of the pocket that are well defined in high-affinity PX domains are highly mobile in SNX1. Some of this mobility is lost upon binding PI(3)P. The C-terminal domain of SNX1 is a long helical dimer that localizes to vesicles but not to the early endosome antigen-1-containing vesicles where endogenous SNX1 resides. Thus, the obligate dimerization of SNX1 that is driven by the C-terminal domain creates a high-affinity PI binding species that properly targets the holo protein to endosomes.
==About this Structure==
==About this Structure==
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2I4K 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=2I4K OCA].
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2I4K 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=2I4K OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Gill, G.N.]]
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[[Category: Gill, G N.]]
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[[Category: Hounslow, A.M.]]
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[[Category: Hounslow, A M.]]
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[[Category: Lazar, C.S.]]
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[[Category: Lazar, C S.]]
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[[Category: Waltho, J.P.]]
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[[Category: Waltho, J P.]]
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[[Category: Watson, M.J.]]
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[[Category: Watson, M J.]]
[[Category: Zhong, Q.]]
[[Category: Zhong, Q.]]
[[Category: 3 alpha helices]]
[[Category: 3 alpha helices]]
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[[Category: proline rich loop]]
[[Category: proline rich loop]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:40:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:48:59 2008''

Revision as of 15:49, 21 February 2008


2i4k

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Solution Structure of the PX domain of Sorting Nexin 1

Overview

The sorting nexin (SNX) family of proteins is characterized by sequence-related phox homology (PX) domains. A minority of PX domains bind with high affinity to phosphatidylinositol 3-phosphate [PI(3)P], whereas the majority of PX domains exhibit low affinity that is insufficient to target them to vesicles. SNX1 is located on endosomes, but its low affinity PX domain fails to localize in vivo. The NMR structure of the PX domain of SNX1 reveals an overall fold that is similar to high-affinity PX domains. However, the phosphatidylinositol (PI) binding pocket of the SNX1 PX domain is incomplete; regions of the pocket that are well defined in high-affinity PX domains are highly mobile in SNX1. Some of this mobility is lost upon binding PI(3)P. The C-terminal domain of SNX1 is a long helical dimer that localizes to vesicles but not to the early endosome antigen-1-containing vesicles where endogenous SNX1 resides. Thus, the obligate dimerization of SNX1 that is driven by the C-terminal domain creates a high-affinity PI binding species that properly targets the holo protein to endosomes.

About this Structure

2I4K is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Determinants of the endosomal localization of sorting nexin 1., Zhong Q, Watson MJ, Lazar CS, Hounslow AM, Waltho JP, Gill GN, Mol Biol Cell. 2005 Apr;16(4):2049-57. Epub 2005 Jan 26. PMID:15673616

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