2ftu
From Proteopedia
(New page: 200px<br /> <applet load="2ftu" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ftu" /> '''solution structure of domain 3 of RAP'''<br...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2ftu.gif|left|200px]]<br /> | + | [[Image:2ftu.gif|left|200px]]<br /><applet load="2ftu" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2ftu" size=" | + | |
caption="2ftu" /> | caption="2ftu" /> | ||
'''solution structure of domain 3 of RAP'''<br /> | '''solution structure of domain 3 of RAP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The receptor associated protein (RAP) is an antagonist and molecular | + | The receptor associated protein (RAP) is an antagonist and molecular chaperone that binds tightly to low-density lipoprotein receptor family members in the endoplasmic reticulum (ER). After escorting these receptors to the Golgi, RAP dissociates from the receptors. The molecular mechanism of the dissociation has been unknown until now. The solution structure of RAP-D3 domain presented here reveals a striking increase in positively charged residues on the surface of this RAP domain due to protonation of solvent-exposed histidine sidechains as the pH is reduced from a near neutral pH of the ER to the acidic pH of the Golgi. Structure-based mutagenesis studies in vitro and in cells confirm that the protonation of histidine residues as a consequence of the pH changes modulate the binding/release of RAP from LRP. This histidine switch may serve as a general mechanism for regulating cell trafficking events. |
==About this Structure== | ==About this Structure== | ||
| - | 2FTU 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:// | + | 2FTU 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=2FTU OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Lee, D.]] | [[Category: Lee, D.]] | ||
| - | [[Category: Walsh, J | + | [[Category: Walsh, J D.]] |
| - | [[Category: Wang, Y | + | [[Category: Wang, Y X.]] |
[[Category: domain 3; rap; receptor-associated protein]] | [[Category: domain 3; rap; receptor-associated protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:25:03 2008'' |
Revision as of 15:25, 21 February 2008
|
solution structure of domain 3 of RAP
Overview
The receptor associated protein (RAP) is an antagonist and molecular chaperone that binds tightly to low-density lipoprotein receptor family members in the endoplasmic reticulum (ER). After escorting these receptors to the Golgi, RAP dissociates from the receptors. The molecular mechanism of the dissociation has been unknown until now. The solution structure of RAP-D3 domain presented here reveals a striking increase in positively charged residues on the surface of this RAP domain due to protonation of solvent-exposed histidine sidechains as the pH is reduced from a near neutral pH of the ER to the acidic pH of the Golgi. Structure-based mutagenesis studies in vitro and in cells confirm that the protonation of histidine residues as a consequence of the pH changes modulate the binding/release of RAP from LRP. This histidine switch may serve as a general mechanism for regulating cell trafficking events.
About this Structure
2FTU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
RAP uses a histidine switch to regulate its interaction with LRP in the ER and Golgi., Lee D, Walsh JD, Mikhailenko I, Yu P, Migliorini M, Wu Y, Krueger S, Curtis JE, Harris B, Lockett S, Blacklow SC, Strickland DK, Wang YX, Mol Cell. 2006 May 5;22(3):423-30. PMID:16678114
Page seeded by OCA on Thu Feb 21 17:25:03 2008
