1C7C

DEOXY RHB1.1 (RECOMBINANT HEMOGLOBIN)

Summary for 1C7C

• Entry DOI: 10.2210/pdb1c7c/pdb
• Related: 1C7B 1C7D
• Descriptor: PROTEIN (DEOXYHEMOGLOBIN (ALPHA CHAIN)), PROTEIN (DEOXYHEMOGLOBIN (BETA CHAIN)), PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: heme, oxygen delivery vehicle, blood substitute, oxygen storage-transport complex, oxygen storage/transport
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 64712.48

Authors

Brucker, E.A. (deposition date: 2000-02-09, release date: 2000-06-30, Last modification date: 2023-08-09)

Primary citation

Brucker, E.A.
Genetically crosslinked hemoglobin: a structural study.
Acta Crystallogr.,Sect.D, 56:812-816, 2000

PubMed Abstract: The crystal structures of three recombinant human hemoglobins, rHb1. 0, rHb1.1 and rHb1.2, have been determined in the deoxy state at 1.8 A resolution. Two of the three proteins, rHb1.1 and rHb1.2, contain a genetic fusion of the alpha subunits, a one- or two-glycine link, respectively, whereas rHb1.0 does not. The glycine crosslinks, localized between one N- and C--termini pair of the alpha subunits in the deoxy crystalline state, do not perturb the overall tertiary or quaternary or even the local structure of hemoglobin. Therefore, genetic fusion to prevent the dissociation of the hemoglobin tetramer, thereby inhibiting renal clearance based upon molecular size, is a structurally conservative method to stabilize hemoglobin for use as an oxygen-delivery therapeutic.

PubMed: 10930828
DOI: 10.1107/S0907444900006557

Experimental method

X-RAY DIFFRACTION (1.8 Å)