|
|
| Line 1: |
Line 1: |
| [[Image:2d5z.gif|left|200px]] | | {{Seed}} |
| | [[Image:2d5z.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_2d5z| PDB=2d5z | SCENE= }} | | {{STRUCTURE_2d5z| PDB=2d5z | SCENE= }} |
|
| |
|
| '''Crystal structure of T-state human hemoglobin complexed with three L35 molecules'''
| | ===Crystal structure of T-state human hemoglobin complexed with three L35 molecules=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16403522}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16403522 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_16403522}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 32: |
Line 36: |
| [[Category: Hemoglobin]] | | [[Category: Hemoglobin]] |
| [[Category: L35]] | | [[Category: L35]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:45:45 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:20:42 2008'' |