1HGC

HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN

Summary for 1HGC

• Entry DOI: 10.2210/pdb1hgc/pdb
• Descriptor: HEMOGLOBIN (OXY) (ALPHA CHAIN), HEMOGLOBIN (DEOXY) (BETA CHAIN), PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• Functional Keywords: oxygen transport
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 64611.05

Authors

Liddington, R.,Derewenda, Z.,Dodson, E.,Hubbard, R.,Dodson, G. (deposition date: 1991-10-31, release date: 1994-01-31, Last modification date: 2024-05-22)

Primary citation

Liddington, R.,Derewenda, Z.,Dodson, E.,Hubbard, R.,Dodson, G.
High resolution crystal structures and comparisons of T-state deoxyhaemoglobin and two liganded T-state haemoglobins: T(alpha-oxy)haemoglobin and T(met)haemoglobin.
J.Mol.Biol., 228:551-579, 1992

PubMed Abstract: 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.

PubMed: 1453464
DOI: 10.1016/0022-2836(92)90842-8

Experimental method

X-RAY DIFFRACTION (2.1 Å)