α-globin

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Hemoglobin α subunit
Hemoglobin α subunit
Hb dimer: front α subunit as a cartoon model with heme (red, as VDW model), rear β subunit as rods, according to PDB  1GZX

Existing structural data : UniProt entry

Mass / length primary structure 16,000 daltons , 141 amino acids
Cofactor Hamm
Identifier
Gene name (s) HBA1 , HBA2
External IDs
Occurrence
Homology family Beta-2 globin
Parent taxon Vertebrates

α-globin , alpha-globin , or hemoglobin alpha chain is a protein from the globins family whose 142 amino acid long polypeptide chain binds a heme as a cofactor and is part of the protein complex of hemoglobins in vertebrates , the hemoglobin subunit alpha ( HBA1 , HBA2 ).

function

The human hemoglobin α1 gene cluster is located on chromosome 16 , comprises 30 kilobases and seven loci : 5'- ζ - pseudo-ζ - μ - pseudo-α-1 - α-2 - α-1 - θ - 3 '. The coding sequences for α-2 ( HBA2 ) and α-1 (HBA1) are identical. These genes differ only slightly in the 5 ' untranslated region and the introns , but they differ significantly in the 3' untranslated region. Two α chains plus two β chains form hemoglobin A (HbA), which in normal adult life comprises approximately 97% of total hemoglobin ; Alpha chains in combination with delta chains form HbA-2, which together with HbF (“fetal hemoglobin”) makes up the remaining 3% of the hemoglobin in adults. Alpha thalassemia results from the deletion of one of the alpha genes as well as deletion of both HBA2 and HBA1; some α-thalassemias without deletion have been reported.

interaction

α-globin has protein-protein interaction with β-globin .

Individual evidence

  1. ↑ Entrez Gene: HBA1 hemoglobin, alpha 1 . Retrieved May 20, 2012.
  2. ↑ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE: A human protein-protein interaction network: a resource for annotating the proteome . In: Cell . 122, No. 6, September 2005, pp. 957-68. doi : 10.1016 / j.cell.2005.08.029 . PMID 16169070 .
  3. ↑ Shaanan B: Structure of human oxyhaemoglobin at 2.1 A resolution . In: J. Mol. Biol. . 171, No. 1, November 1983, pp. 31-59. doi : 10.1016 / S0022-2836 (83) 80313-1 . PMID 6644819 .

Web links

literature

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