2) What\'s known about the biological role of that domain in your protein? For e

Question

2) What's known about the biological role of that domain in your protein? For example, how mutations in that domain cause interesting phenotypes. Or, if that domain is essential to the function, for example, it's the ATP-binding domain in a kinase

FASTA hemoglobin subunit beta [Homo sapiensl NCBI Reference Sequence: NP 000509.1 GenPept dentical Proteins Graphics >NP 0 0 0509.1 7-146 hemoglobin subunit beta Homo sapiens EEKSAVTAL WGKVNVDEVGGEALGRLLVVYPWTORFFESFGDLSTPDAVMGNPKVKAHGK KVLGAFSDGL AHLDNIKGTFATLSELHC DKLHVDPENFRL LGNVLVCVLAHHFG KEFTPPVOAAY QKVVAGVANALAHKY Send to

Explanation / Answer

1) Haemoglobin subunit beta is a globin protein, which along with alpha globin (HBA), makes up the most common form of haemoglobin in adult humans, the HbA. It is 146 amino acids long and has a molecular weight of 15,867 Da. Normal adult human HbA is a heterotetramer consisting of two alpha chains and two beta chains. The specific base sequence for these amino acids is: GTG/CAC/CTG/ACT/CCT/GAG.

2) The alpha (HBA) and beta (HBB) loci determine the structure of the 2 types of polypeptide chains in adult hemoglobin, Hb A. The normal adult hemoglobin tetramer consists of two alpha chains and two beta chains. Mutant beta globin causes sickle cell anemia. Absence of beta chain causes beta-zero-thalassemia. Reduced amounts of detectable beta globin causes beta-plus-thalassemia. The order of the genes in the beta-globin cluster is 5'-epsilon -- gamma-G -- gamma-A -- delta -- beta--3'.

Biological role:

contributes to haptoglobin binding PubMed contributes_to peroxidase activity PubMed heme binding hemoglobin binding PubMed iron ion binding oxygen binding PubMed oxygen transporter activity PubMed protein binding

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