| Differences between HbS (sickle) and HbA (adult) |
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In images below, amino acid residues of HbA are highlighted that are either mutated in HbS or participate in the deoxyHbS polmerization process . These residues include b-Glu6 of HbA, which is mutated b-Val6 in the HbS, and b-Phe85 and b-Leu88 which form the hydrophobic pocket for binding theb-Val6 sidechain.
| Instructions: If not already visible in the lower frame, load the X-ray structures for oxyHbA and deoxyHbA . | |
1. Spacefilled images of deoxyHbA and oxyHbA as viewed between the two (dark and light red) b -subunits. | |
| Color Scheme The b-Glu6 residues of HbA (mutated to b-Val6 in sHbA) are colored green. The | |
| 2. Closeup of the b-b interface (dark and light red) with labeled residues and featuring HbA b-Glu6 (green) and the HbS b-Val6 binding pockets created by b-Phe58 and b-Leu88 (yellow). | |
| 3. Distance between the HbS b-Val6 binding pockets in deoxyHb and oxyHb. | |
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© Duane W.
Sears
Revised: July 27, 1998
-Val6 binding pockets created by b-Phe85 and b-Leu88 on the surface of the two b-chains of HbA, or on the g-chain of HbF, are colored yellow.