v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | This entry is the domain 2 (D2) of receptor-associated protein, RAP, also known as alpha-2-macroglobulin receptor-associated protein. RAP is a three domain ER (endoplasmic reticulum)-resident protein that is a chaperone for the LRP (low-density lipoprotein receptor-related protein). RAP is an antagonist and a specialized chaperone that binds tightly to members of the low-density lipoprotein (LDL) receptor family and prevents them from associating with other ligands [ ].D2, along with RAP domain 1 (D1), is essential for blocking low-density lipoprotein receptor-related protein (LRP) from binding of certain ligands, such as alpha2-macroglobulin; D1 and D2 each bind LRP weakly but the tandem D1D2 binds much more tightly to the second and the fourth ligand-binding clusters present on LRP, suggesting the avidity effects arising from amino acid residues contributed from each domain [ ]. Also, RAP has regions that interact weakly with heparin, one located in D2 and two located in D3. The double module of complement type repeats, CR56, of LRP binds many ligands including alpha2-macroglobulin, which promotes the catabolism of the Abeta-peptide implicated in Alzheimer's disease []. |
| Short Name | RAP_D2 |