(a) The 2,3-BPG binding site is located in the central cavity of the adult hemoglobin (HbA) tetramer between the two B-globin chains (see also Figure 7.22). Hls 143 Ser 143 In fetal Hb (b) Zoom in on the central cavity, which is lined with eight positively charged groups (highlighted in yellow) that favorably bind the negatively charged 2,3-BPG molecule. Note the His residues (8143) that are replaced by Ser in fetal hemoglobin (cyan arrows and dashed ovals). A FIGURE 7.29 Binding of 2,3-bisphosphoglycerate to deoxyhemo- globin. Human hemoglobin colored as in Figure 7.22. PDB ID: 1b86.

Biochemistry
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ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
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The mutation in hemoglobin at β82 Lys→Asp results in lowered O2-binding
affinity compared to normal hemoglobin. β82 is one of the residues that
lines the 2,3-BPG binding site (as shown; β82 is adjacent to His 143). Based on the location of this residue and the differences between Lys and Asp, suggest a rationale for the observed reduction in O2-binding affinity.

(a) The 2,3-BPG binding site is located in the central cavity of the
adult hemoglobin (HbA) tetramer between the two B-globin chains
(see also Figure 7.22).
Hls 143 Ser 143 In fetal Hb
(b) Zoom in on the central cavity, which is lined with eight positively
charged groups (highlighted in yellow) that favorably bind the
negatively charged 2,3-BPG molecule. Note the His residues (8143)
that are replaced by Ser in fetal hemoglobin (cyan arrows and
dashed ovals).
A FIGURE 7.29 Binding of 2,3-bisphosphoglycerate to deoxyhemo-
globin. Human hemoglobin colored as in Figure 7.22. PDB ID: 1b86.
Transcribed Image Text:(a) The 2,3-BPG binding site is located in the central cavity of the adult hemoglobin (HbA) tetramer between the two B-globin chains (see also Figure 7.22). Hls 143 Ser 143 In fetal Hb (b) Zoom in on the central cavity, which is lined with eight positively charged groups (highlighted in yellow) that favorably bind the negatively charged 2,3-BPG molecule. Note the His residues (8143) that are replaced by Ser in fetal hemoglobin (cyan arrows and dashed ovals). A FIGURE 7.29 Binding of 2,3-bisphosphoglycerate to deoxyhemo- globin. Human hemoglobin colored as in Figure 7.22. PDB ID: 1b86.
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