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PDBsum entry 1ch4
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Oxygen transport
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PDB id
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1ch4
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of a protein with an artificial exon-Shuffling, Module m4-Substituted chimera hemoglobin beta alpha, At 2.5 a resolution.
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Authors
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T.Shirai,
M.Fujikake,
T.Yamane,
K.Inaba,
K.Ishimori,
I.Morishima.
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Ref.
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J Mol Biol, 1999,
287,
369-382.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of the homotetramer of a chimera beta alpha-subunit of
human hemoglobin was refined at 2.5 A resolution. The chimera subunit was
constructed by replacing an exon-encoded module M4 of the beta-subunit with that
of the alpha-subunit, simulating an exon-shuffling event. The implanted module
M4 retained the native alpha-subunit structure, while module M3 was disturbed
around the site where a new type of intron was recently found. Some of the
residues were found in alternative conformations that avoid steric hindrance at
the subunit interface. The modules are modestly rigid in their backbone
structures by using side-chains to compensate for interface incompatibility.
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Figure 4.
Figure 4. A stereo view of the side-chain and heme group
packing around fine tuning site Val133 (H11). The structures of
α-subunit (gray), β-subunit (blue) and chimera subunit
(yellow) are superimposed.
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Figure 6.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(1999,
287,
369-382)
copyright 1999.
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Secondary reference #1
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Title
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Design, Construction, Crystallization, And preliminary X-Ray studies of a fine-Tuning mutant (f133V) of module-Substituted chimera hemoglobin.
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Authors
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T.Shirai,
M.Fujikake,
T.Yamane,
K.Inaba,
K.Ishimori,
I.Morishima.
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Ref.
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Proteins, 1998,
32,
263-267.
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PubMed id
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