Abstract
Structural analysis of a fast-moving hemoglobin variant, present in three members of a Qatari family, identified a Val → Glu substitution at position 1 (NA1) of the β-chain. The introduction of this glutamic acid residue prevents the removal of the initiator methione, thus extending the N-terminus by one residue to Met-Glu-His-Leu-Thr-. THe methionine residue is blocked by an as yet not completely identified molecule. The presence of the variant in a heterozygote does not have clinical consequences.
Original language | English (US) |
---|---|
Pages (from-to) | 257-260 |
Number of pages | 4 |
Journal | Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular |
Volume | 831 |
Issue number | 2 |
DOIs | |
State | Published - Oct 4 1985 |
Keywords
- (Human)
- Amino acid sequence
- Blocking group
- Hemoglobin variant
- Methionine
- N-terminal
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology