2ftu
From Proteopedia
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[[Image:2ftu.gif|left|200px]] | [[Image:2ftu.gif|left|200px]] | ||
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'''solution structure of domain 3 of RAP''' | '''solution structure of domain 3 of RAP''' | ||
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[[Category: Walsh, J D.]] | [[Category: Walsh, J D.]] | ||
[[Category: Wang, Y X.]] | [[Category: Wang, Y X.]] | ||
| - | [[Category: | + | [[Category: Domain 3]] |
| - | [[Category: | + | [[Category: Rap]] |
| - | [[Category: | + | [[Category: Receptor-associated protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:18:08 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 01:18, 4 May 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 Sun May 4 04:18:08 2008
