2FTU
solution structure of domain 3 of RAP
Summary for 2FTU
| Entry DOI | 10.2210/pdb2ftu/pdb |
| Related | 2FFT 2FFV |
| Descriptor | Alpha-2-macroglobulin receptor-associated protein, domain 3 (1 entity in total) |
| Functional Keywords | domain 3; rap; receptor-associated protein, lipid binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Endoplasmic reticulum: P30533 |
| Total number of polymer chains | 1 |
| Total formula weight | 13881.46 |
| Authors | Lee, D.,Walsh, J.D.,Wang, Y.-X. (deposition date: 2006-01-24, release date: 2006-05-09, Last modification date: 2024-05-29) |
| Primary citation | Lee, D.,Walsh, J.D.,Mikhailenko, I.,Yu, P.,Migliorini, M.,Wu, Y.,Krueger, S.,Curtis, J.E.,Harris, B.,Lockett, S.,Blacklow, S.C.,Strickland, D.K.,Wang, Y.X. RAP uses a histidine switch to regulate its interaction with LRP in the ER and Golgi. Mol.Cell, 22:423-430, 2006 Cited by PubMed Abstract: 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. PubMed: 16678114DOI: 10.1016/j.molcel.2006.04.011 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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