6HBW
Crystal structure of deoxy-human hemoglobin beta6 glu->trp
Summary for 6HBW
| Entry DOI | 10.2210/pdb6hbw/pdb |
| Descriptor | PROTEIN (HEMOGLOBIN ALPHA 1), PROTEIN (HEMOGLOBIN BETA), PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total) |
| Functional Keywords | oxygen transport, hemoglobin, oxygen storage-transport complex, oxygen storage/transport |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 64661.25 |
| Authors | Harrington, D.J.,Adachi, K.,Royer Jr., W.E. (deposition date: 1998-09-10, release date: 1998-09-16, Last modification date: 2023-09-20) |
| Primary citation | Harrington, D.J.,Adachi, K.,Royer Jr., W.E. Crystal structure of deoxy-human hemoglobin beta6 Glu --> Trp. Implications for the structure and formation of the sickle cell fiber. J.Biol.Chem., 273:32690-32696, 1998 Cited by PubMed Abstract: An atomic-level understanding of the interactions between hemoglobin molecules that contribute to the formation of pathological fibers in sickle cell disease remains elusive. By exploring crystal structures of mutant hemoglobins with altered polymerization properties, insight can be gained into sickle cell hemoglobin (HbS) polymerization. We present here the 2.0-A resolution deoxy crystal structure of human hemoglobin mutated to tryptophan at the beta6 position, the site of the glutamate --> valine mutation in HbS. Unlike leucine and isoleucine, which promote polymerization relative to HbS, tryptophan inhibits polymerization. Our results provide explanations for the altered polymerization properties and reveal a fundamentally different double strand that may provide a model for interactions within a fiber and/or interactions leading to heterogeneous nucleation. PubMed: 9830011DOI: 10.1074/jbc.273.49.32690 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report
