The conserved Phe GH5 of importance for hemoglobin intersubunit contact is mutated in gadoid fish.

ABSTRACT:

Background

Functionality of the tetrameric hemoglobin molecule seems to be determined by a few amino acids located in key positions. Oxygen binding encompasses structural changes at the interfaces between the α1β2 and α2β1 dimers, but also subunit interactions are important for the oxygen binding affinity and stability. The latter packing contacts include the conserved Arg B12 interacting with Phe GH5, which is replaced by Leu and Tyr in the αA and αD chains, respectively, of birds and reptiles.

Results

Searching all known hemoglobins from a variety of gnathostome species (jawed vertebrates) revealed the almost invariant Arg B12 coded by the AGG triplet positioned at an exon-intron boundary. Rare substitutions of Arg B12 in the gnathostome β globins were found in pig, tree s

SUBMITTER: Andersen O 

PROVIDER: S-EPMC3998052 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature