Structures of R- and T-state hemoglobin Bassett: elucidating the structural basis for the low oxygen affinity of a mutant hemoglobin

Safo, M.K.; Abdulmalik, O.; Lin, H.-R.; Asakura, T.; Abraham, D.J.

doi:10.1107/S0907444904030501

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 1
Stereo figure of the α1β2 dimer interface of R-state Hb. The residues are shown in ribbons and/or ball-and-stick representation. Water molecules are shown as spheres, while hydrogen bonds are represented by dashed lines. (a) Superposition of the α1β2 dimer interface of Hb Bassett (red) and HbA (yellow). The structures were superimposed using the invariant α1β1 dimer (C^α residues) on the BGH frame (see text). (b) The α1β2 dimer interface of Hb Bassett showing intersubunit hydrogen-bonding interactions (see Table 2

for values). The α1-subunit and β2-subunit are in magenta and cyan, respectively. O and N atoms are in red and blue, respectively. Some side chains are omitted for clarity. The figures were generated with MOLSCRIPT (Kraulis, 1991

) and RASTER3D (Merritt & Murphy, 1994

) and labeled with SHOWCASE.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 61| Part 2| January 2005| Pages 156-162

doi:10.1107/S0907444904030501

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