Summary for 3KQ0
| Entry DOI | 10.2210/pdb3kq0/pdb |
| Related | 3BX6 |
| Descriptor | Alpha-1-acid glycoprotein 1, (2R)-2,3-dihydroxypropyl acetate, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | plasma protein, glycoprotein, polymorphism, acute phase protein, secreted, pyrrolidone carboxylic acid, lipocalin, signaling protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 22850.86 |
| Authors | Schiefner, A.,Schonfeld, D.L.,Ravelli, R.B.G.,Mueller, U.,Skerra, A. (deposition date: 2009-11-17, release date: 2010-02-02, Last modification date: 2024-11-20) |
| Primary citation | Schonfeld, D.L.,Ravelli, R.B.,Mueller, U.,Skerra, A. The 1.8-A crystal structure of alpha1-acid glycoprotein (Orosomucoid) solved by UV RIP reveals the broad drug-binding activity of this human plasma lipocalin. J.Mol.Biol., 384:393-405, 2008 Cited by PubMed Abstract: Alpha(1)-acid glycoprotein (AGP) is an important drug-binding protein in human plasma and, as an acute-phase protein, it has a strong influence on pharmacokinetics and pharmacodynamics of many pharmaceuticals. We report the crystal structure of the recombinant unglycosylated human AGP at 1.8 A resolution, which was solved using the new method of UV-radiation-damage-induced phasing (UV RIP). AGP reveals a typical lipocalin fold comprising an eight-stranded beta-barrel. Of the four loops that form the entrance to the ligand-binding site, loop 1, which connects beta-strands A and B, is among the longest observed so far and exhibits two full turns of an alpha-helix. Furthermore, it carries one of the five N-linked glycosylation sites, while a second one occurs underneath the tip of loop 2. The branched, partly hydrophobic, and partly acidic cavity, together with the presumably flexible loop 1 and the two sugar side chains at its entrance, explains the diverse ligand spectrum of AGP, which is known to vary with changes in glycosylation pattern. PubMed: 18823996DOI: 10.1016/j.jmb.2008.09.020 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report
