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PDBsum entry 1c7c
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protein ligands Protein-protein interface(s) links
Oxygen storage/transport PDB id
1c7c

 

 

 

 

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Contents
Protein chains
283 a.a.
146 a.a. *
Ligands
HEM ×4
Waters ×322
* Residue conservation analysis
PDB id:
1c7c
Name: Oxygen storage/transport
Title: Deoxy rhb1.1 (recombinant hemoglobin)
Structure: Protein (deoxyhemoglobin (alpha chain)). Chain: a. Engineered: yes. Mutation: yes. Protein (deoxyhemoglobin (beta chain)). Chain: b, d. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell: red blood cell. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
Biol. unit: Trimer (from PQS)
Resolution:
1.80Å     R-factor:   0.176     R-free:   0.227
Authors: E.A.Brucker
Key ref:
E.A.Brucker (2000). Genetically crosslinked hemoglobin: a structural study. Acta Crystallogr D Biol Crystallogr, 56, 812-816. PubMed id: 10930828 DOI: 10.1107/S0907444900006557
Date:
09-Feb-00     Release date:   30-Jun-00    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P69905  (HBA_HUMAN) -  Hemoglobin subunit alpha from Homo sapiens
Seq:
Struc: 		142 a.a.
283 a.a.*
Protein chains
Pfam   ArchSchema ?
P68871  (HBB_HUMAN) -  Hemoglobin subunit beta from Homo sapiens
Seq:
Struc: 		147 a.a.
146 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 

 
DOI no: 10.1107/S0907444900006557 Acta Crystallogr D Biol Crystallogr 56:812-816 (2000)
PubMed id: 10930828  
 
 
Genetically crosslinked hemoglobin: a structural study.
E.A.Brucker.
 
  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.
 
  Selected figure(s)  
 
Figure 2.
Figure 2 Overlay of HbA[0], rHb1.1 and rHb1.2. Stereoview includes the subunit N- and C-termini (glycine crosslink) region; HbA[0] (Protein Data Bank entry 2hhb; Fermi et al., 1984[Fermi, G., Perutz, M. F., Shaanan, B. & Fourme, R. (1984). J. Mol. Biol. 175, 159-174.]) with associated text is drawn in black, rHb1.1 in light gray and rHb1.2 in dark gray. Coordinates were superposed by overlaying the C^ atoms of the hemoglobins.
 
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2000, 56, 812-816) copyright 2000.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
15383027 P.W.Buehler, and A.I.Alayash (2004).
Toxicities of hemoglobin solutions: in search of in-vitro and in-vivo model systems.
  Transfusion, 44, 1516-1530.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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