1LRE
RECEPTOR ASSOCIATED PROTEIN (RAP) DOMAIN 1, NMR, 20 STRUCTURES
Summary for 1LRE
| Entry DOI | 10.2210/pdb1lre/pdb |
| Descriptor | RECEPTOR-ASSOCIATED PROTEIN (1 entity in total) |
| Functional Keywords | alpha2-macroglobulin receptor associated protein, low density lipoprotein receptor family associated protein, ldlr family associated protein, helix bundle, cell surface protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Endoplasmic reticulum: P30533 |
| Total number of polymer chains | 1 |
| Total formula weight | 9536.01 |
| Authors | Nielsen, P.R.,Poulsen, F.M. (deposition date: 1997-05-08, release date: 1997-08-20, Last modification date: 2024-05-22) |
| Primary citation | Nielsen, P.R.,Ellgaard, L.,Etzerodt, M.,Thogersen, H.C.,Poulsen, F.M. The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein. Proc.Natl.Acad.Sci.USA, 94:7521-7525, 1997 Cited by PubMed Abstract: The three-dimensional structure of the N-terminal domain (residues 18-112) of alpha2-macroglobulin receptor-associated protein (RAP) has been determined by NMR spectroscopy. The structure consists of three helices composed of residues 23-34, 39-65, and 73-88. The three helices are arranged in an up-down-up antiparallel topology. The C-terminal 20 residues were shown not to be in a well defined conformation. A structural model for the binding of RAP to the family of low-density lipoprotein receptors is proposed. It defines a role in binding for both the unordered C terminus and the structural scaffold of the core structure. Pathogenic epitopes for the rat disease Heymann nephritis, an experimental model of human membranous glomerulonephritis, have been identified in RAP and in the large endocytic receptor gp330/megalin. Here we provide the three-dimensional structure of the pathogenic epitope in RAP. The amino acid residues known to form the epitope are in a helix-loop-helix conformation, and from the structure it is possible to rationalize the published results obtained from studies of fragments of the N-terminal domain. PubMed: 9207124DOI: 10.1073/pnas.94.14.7521 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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