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PDBsum entry 6kye
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Oxygen transport
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PDB id
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6kye
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Contents |
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(+ 0 more)
140 a.a.
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(+ 0 more)
146 a.a.
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PDB id:
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Oxygen transport
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Title:
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The crystal structure of recombinant human adult hemoglobin
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Structure:
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Hemoglobin subunit alpha. Chain: a, c, e, g, i, k. Synonym: alpha-globin,hemoglobin alpha chain. Engineered: yes. Hemoglobin subunit beta. Chain: b, d, f, h, j, l. Synonym: beta-globin,hemoglobin beta chain. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: hba1, hba2. Expressed in: komagataella phaffii gs115. Expression_system_taxid: 644223. Gene: hbb.
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Resolution:
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2.28Å
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R-factor:
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0.228
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R-free:
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0.268
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Authors:
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K.Kihira,R.Funaki,W.Okamoto,C.Endo,Y.Morita,T.Komatsu
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Key ref:
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R.Funaki
et al.
(2020).
Genetically engineered haemoglobin wrapped covalently with human serum albumins as an artificial O2 carrier.
J Mater Chem B,
8,
1139-1145.
PubMed id:
DOI:
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Date:
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18-Sep-19
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Release date:
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01-Jan-20
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PROCHECK
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Headers
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References
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DOI no:
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J Mater Chem B
8:1139-1145
(2020)
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PubMed id:
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Genetically engineered haemoglobin wrapped covalently with human serum albumins as an artificial O2 carrier.
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R.Funaki,
W.Okamoto,
C.Endo,
Y.Morita,
K.Kihira,
T.Komatsu.
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ABSTRACT
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We describe the synthesis and O2 affinity of genetically engineered
human adult haemoglobin (rHbA) wrapped covalently with recombinant human serum
albumins (rHSAs) as an artificial O2 carrier used for a completely
synthetic red blood cell (RBC) substitute. Wild-type rHbA [rHbA(wt)] expressed
in yeast species Pichia pastoris shows an identical amino acid sequence and
three-dimensional structure to those of native HbA. It is particularly
interesting that two orientations of the prosthetic haem group in rHbA(wt) were
aligned by gentle heating in the natural form. Covalent wrapping of rHbA(wt)
with three rHSAs conferred a core-shell structured haemoglobin-albumin cluster:
rHbA(wt)-rHSA3. Three variant clusters containing an rHbA mutant core
were also created: Leu-β28 → Phe, Leu-β28 → Trp, and Leu-β28 →
Tyr/His-β63 → Gln. Replacement of Leu-β28 with Trp decreased the distal
space in the haem pocket, thereby yielding a cluster with moderately low
O2 affinity which is nearly the same as that of human RBC.
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Links
