β-globin

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Β-globin
Β-globin
Structure of β-globin in the homotetramer
Identifier
Gene name (s) HBB; CD113t-C; beta globin

β-globin , beta-globin , or hemoglobin beta chain is a protein from the family of globins , the 147 amino acids long polypeptide chain , a heme as a cofactor binds and so as hemoglobin subunit beta ( HBB ) part of hemoglobin - protein complexes in vertebrates is. In adults, the most common form of hemoglobin used to transport oxygen is a tetramer made up of two beta and two alpha chains (HBA), the so-called adult hemoglobin A (HbA (1) - α 2 β 2 ).

Locate

When human β-globin (HBB) is from HBB - gene encodes the gene cluster of the β-globin locus ( 5 '- hbe1 - hbg2 - hbg1 - HBD -3 HBB -' ) on chromosome 11 is located. The expression of these very similar genes is controlled here via a common locus control region (LCR) and is development-dependently different. Depending on the development phase or cell environment, protein biosynthesis can be initiated by the corresponding ε , γ , δ or β globins.

The proteins formed differ from each other only in a few amino acids of their 147 AA long chain; however, the hemoglobins made up of them show differences in oxygen - binding capacity . While epsilon - (for embryonic hemoglobin ) and gamma- globin (for fetal hemoglobin , HbF) are formed prenatally , after birth it is usually mainly beta - and less often delta- globin (for adult hemoglobin, HbA (1) - α 2 β 2 or HbA 2 - α 2 δ 2 ).

Diseases

Mutations in the gene for β-globin are the cause of a disease of red blood cells with typical changes in their shape, sickle cell anemia . The lack of beta chains causes thalassemia major (also β 0 thalassemia); In thalassemia minor (also ß + thalassemia), the amount of detectable β-globin is reduced and the symptoms are less pronounced.

Interactions

HBB shows protein-protein interaction with α-globin .

Individual evidence

  1. ↑ a b Entrez Gene: HBB hemoglobin, beta . Retrieved May 11, 2012.
  2. ↑ Entrez Gene: HBE1 hemoglobin, epsilon 1 . Retrieved May 19, 2012.
  3. ↑ Levings PP, Bungert J: The human beta-globin locus control region . In: Eur. J. Biochem. . 269, No. 6, March 2002, pp. 1589-99. doi : 10.1046 / j.1432-1327.2002.02797.x . PMID 11895428 .
  4. ↑ Higgs DR, Vickers MA, Wilkie AO, Pretorius IM, Jarman AP, Weatherall DJ: A review of the molecular genetics of the human alpha-globin gene cluster . In: Blood . 73, No. 5, May 1989, pp. 1081-104. PMID 2649166 .
  5. ↑ Ulrich Stelzl, Worm Uwe, Lalowski Maciej, Haenig Christian, Brembeck Felix H, Goehler Heike, Stroedicke Martin, Zenkner Martina, Schoenherr Anke, Koeppen Susanne, Timm Jan, Mintzlaff Sascha, Abraham Claudia, Bock Nicole, Kietzmann Silvia, Goedde Astrid, Toksöz Engin, Droege Anja, Krobitsch Sylvia, Korn Bernhard, Birchmeier Walter, Lehrach Hans, Wanker Erich E: A human protein-protein interaction network: a resource for annotating the proteome . In: Cell . 122, No. 6, United States, September 2005, pp. 957-68. doi : 10.1016 / j.cell.2005.08.029 . PMID 16169070 .
  6. ↑ B Shaanan: Structure of human oxyhaemoglobin at 2.1 A resolution . In: J. Mol. Biol. . 171, No. 1, ENGLAND, November 1983, pp. 31-59. doi : 10.1016 / S0022-2836 (83) 80313-1 . PMID 6644819 .

literature

  • Higgs DR, Vickers MA, Wilkie AO, et al. : A review of the molecular genetics of the human alpha-globin gene cluster. . In: Blood . 73, No. 5, 1989, pp. 1081-104. PMID 2649166 .
  • Giardina B, Messana I, Scatena R, Castagnola M: The multiple functions of hemoglobin. . In: Crit. Rev. Biochem. Mol. Biol . 30, No. 3, 1995, pp. 165-96. doi : 10.3109 / 10409239509085142 . PMID 7555018 .
  • Salzano AM, Carbone V, Pagano L, et al. : Hb Vila Real [beta36 (C2) Pro -> His] in Italy: characterization of the amino acid substitution and the DNA mutation. . In: Hemoglobin . 26, No. 1, 2002, pp. 21-31. doi : 10.1081 / HEM-120002937 . PMID 11939509 .
  • Frischknecht H, Dutly F: A 65 bp duplication / insertion in exon II of the beta globin gene causing beta0-thalassemia. . In: Haematologica . 92, No. 3, 2007, pp. 423-4. doi : 10.3324 / haematol.10785 . PMID 17339197 .