2D60
Crystal structure of deoxy human hemoglobin complexed with two L35 molecules
Summary for 2D60
| Entry DOI | 10.2210/pdb2d60/pdb |
| Related | 2D5X 2D5Z |
| Descriptor | Hemoglobin alpha subunit, Hemoglobin beta subunit, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total) |
| Functional Keywords | hemoglobin, l35, allosteric effector, crystal sructure, oxygen storage-transport complex, oxygen storage/transport |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 65313.50 |
| Authors | Yokoyama, T.,Neya, S.,Tsuneshige, A.,Yonetani, T.,Park, S.Y.,Tame, J.R. (deposition date: 2005-11-08, release date: 2006-03-07, Last modification date: 2024-03-13) |
| Primary citation | Yokoyama, T.,Neya, S.,Tsuneshige, A.,Yonetani, T.,Park, S.Y.,Tame, J.R. R-state haemoglobin with low oxygen affinity: crystal structures of deoxy human and carbonmonoxy horse haemoglobin bound to the effector molecule L35 J.Mol.Biol., 356:790-801, 2006 Cited by PubMed Abstract: Although detailed crystal structures of haemoglobin (Hb) provide a clear understanding of the basic allosteric mechanism of the protein, and how this in turn controls oxygen affinity, recent experiments with artificial effector molecules have shown a far greater control of oxygen binding than with natural heterotropic effectors. Contrary to the established text-book view, these non-physiological compounds are able to reduce oxygen affinity very strongly without switching the protein to the T (tense) state. In an earlier paper we showed that bezafibrate (BZF) binds to a surface pocket on the alpha subunits of R state Hb, strongly reducing the oxygen affinity of this protein conformation. Here we report the crystallisation of Hb with L35, a related compound, and show that this binds to the central cavity of both R and T state Hb. The mechanism by which L35 reduces oxygen affinity is discussed, in relation to spectroscopic studies of effector binding. PubMed: 16403522DOI: 10.1016/j.jmb.2005.12.018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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