1hgc: Difference between revisions
New page: left|200px<br /> <applet load="1hgc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hgc, resolution 2.1Å" /> '''HIGH RESOLUTION CRYS... |
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==Overview== | ==Overview== | ||
The origin of co-operativity in haemoglobin (Hb) resides in the reduced, affinity of the T-state. T-state Hb crystals grown from polyethyleneglycol, can be liganded without the molecule switching to the R high affinity, state. X-ray analysis of T-state alpha-oxy Hb and T-state met Hb has, identified the structural basis for reduced affinity. The nature of the, chemical tension at the haem environment is different in the alpha and, beta haems. There are small but definite structural changes associated, with ligation in the T-state: these prove to be mostly in the same, direction as the larger changes that occur in the T-->R transition. | The origin of co-operativity in haemoglobin (Hb) resides in the reduced, affinity of the T-state. T-state Hb crystals grown from polyethyleneglycol, can be liganded without the molecule switching to the R high affinity, state. X-ray analysis of T-state alpha-oxy Hb and T-state met Hb has, identified the structural basis for reduced affinity. The nature of the, chemical tension at the haem environment is different in the alpha and, beta haems. There are small but definite structural changes associated, with ligation in the T-state: these prove to be mostly in the same, direction as the larger changes that occur in the T-->R transition. | ||
==Disease== | |||
Known diseases associated with this structure: Erythremias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Erythremias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Erythrocytosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], HPFH, deletion type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Heinz body anemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Heinz body anemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Heinz body anemias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Hemoglobin H disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Hypochromic microcytic anemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Methemoglobinemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Methemoglobinemias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Sickle cell anemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Thalassemia, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Thalassemia-beta, dominant inclusion-body OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Thalassemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Thalassemias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]] | |||
==About this Structure== | ==About this Structure== | ||
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[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
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Revision as of 18:11, 12 November 2007
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HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN
OverviewOverview
The origin of co-operativity in haemoglobin (Hb) resides in the reduced, affinity of the T-state. T-state Hb crystals grown from polyethyleneglycol, can be liganded without the molecule switching to the R high affinity, state. X-ray analysis of T-state alpha-oxy Hb and T-state met Hb has, identified the structural basis for reduced affinity. The nature of the, chemical tension at the haem environment is different in the alpha and, beta haems. There are small but definite structural changes associated, with ligation in the T-state: these prove to be mostly in the same, direction as the larger changes that occur in the T-->R transition.
DiseaseDisease
Known diseases associated with this structure: Erythremias, alpha- OMIM:[141800], Erythremias, beta- OMIM:[141900], Erythrocytosis OMIM:[141850], HPFH, deletion type OMIM:[141900], Heinz body anemia OMIM:[141850], Heinz body anemias, alpha- OMIM:[141800], Heinz body anemias, beta- OMIM:[141900], Hemoglobin H disease OMIM:[141850], Hypochromic microcytic anemia OMIM:[141850], Methemoglobinemias, alpha- OMIM:[141800], Methemoglobinemias, beta- OMIM:[141900], Sickle cell anemia OMIM:[141900], Thalassemia, alpha- OMIM:[141850], Thalassemia-beta, dominant inclusion-body OMIM:[141900], Thalassemias, alpha- OMIM:[141800], Thalassemias, beta- OMIM:[141900]
About this StructureAbout this Structure
1HGC is a Protein complex structure of sequences from Homo sapiens with HEM and OXY as ligands. Full crystallographic information is available from OCA.
ReferenceReference
High resolution crystal structures and comparisons of T-state deoxyhaemoglobin and two liganded T-state haemoglobins: T(alpha-oxy)haemoglobin and T(met)haemoglobin., Liddington R, Derewenda Z, Dodson E, Hubbard R, Dodson G, J Mol Biol. 1992 Nov 20;228(2):551-79. PMID:1453464
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