| First Author | Doi T | Year | 1993 |
| Journal | J Biol Chem | Volume | 268 |
| Issue | 3 | Pages | 2126-33 |
| PubMed ID | 8380589 | Mgi Jnum | J:42397 |
| Mgi Id | MGI:1095731 | Doi | 10.1016/s0021-9258(18)53971-5 |
| Citation | Doi T, et al. (1993) Charged collagen structure mediates the recognition of negatively charged macromolecules by macrophage scavenger receptors. J Biol Chem 268(3):2126-33 |
| abstractText | Macrophage scavenger receptors mediate the recognition of a wide range of negatively charged macromolecules including modified low density lipoproteins (LDL). Truncated bovine receptors lacking residues 330-342, which include the conserved lysine cluster of a collagen-like domain, were unable to degrade modified LDL in spite of their expression on the cell surface. Substitution of lysine 337 into alanine abolished the acetyl-LDL degradation and binding at 37 degrees C, but did not abolish the 4 degrees C binding. In contrast, substitution of more than 2 lysines in this region are needed to abolish the oxidized LDL degradation and 37 degrees C binding. Based on computational modeling of this domain, we propose that a charged collagen structure containing a lysine cluster forms a positively charged groove which specifically interacts with negatively charged ligands. |
