(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
9th Edition
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
Problem 1P
icon
Related questions
icon
Concept explainers
Question

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.
Expert Solution
trending now

Trending now

This is a popular solution!

steps

Step by step

Solved in 2 steps

Blurred answer
Knowledge Booster
Organ system
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.
Similar questions
Recommended textbooks for you
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman
Lehninger Principles of Biochemistry
Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul…
Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781305961135
Author:
Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:
Cengage Learning
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781305577206
Author:
Reginald H. Garrett, Charles M. Grisham
Publisher:
Cengage Learning
Fundamentals of General, Organic, and Biological …
Fundamentals of General, Organic, and Biological …
Biochemistry
ISBN:
9780134015187
Author:
John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:
PEARSON