Bibliographic Details
| Title: |
Alteration of the α1β2/α2β1 subunit interface contributes to the increased hemoglobin-oxygen affinity of high-altitude deer mice. |
| Authors: |
Noriko Inoguchi, Nobuhiro Mizuno, Seiki Baba, Takashi Kumasaka, Chandrasekhar Natarajan, Jay F Storz, Hideaki Moriyama |
| Source: |
PLoS ONE, Vol 12, Iss 3, p e0174921 (2017) |
| Publisher Information: |
Public Library of Science (PLoS), 2017. |
| Publication Year: |
2017 |
| Collection: |
LCC:Medicine
LCC:Science |
| Subject Terms: |
Medicine, Science |
| More Details: |
BACKGROUND:Deer mice (Peromyscus maniculatus) that are native to high altitudes in the Rocky Mountains have evolved hemoglobins with an increased oxygen-binding affinity relative to those of lowland conspecifics. To elucidate the molecular mechanisms responsible for the evolved increase in hemoglobin-oxygen affinity, the crystal structure of the highland hemoglobin variant was solved and compared with the previously reported structure for the lowland variant. RESULTS:Highland hemoglobin yielded at least two crystal types, in which the longest axes were 507 and 230 Å. Using the smaller unit cell crystal, the structure was solved at 2.2 Å resolution. The asymmetric unit contained two tetrameric hemoglobin molecules. CONCLUSIONS:The analyses revealed that αPro50 in the highland hemoglobin variant promoted a stable interaction between αHis45 and heme that was not seen in the αHis50 lowland variant. The αPro50 mutation also altered the nature of atomic contacts at the α1β2/α2β1 intersubunit interfaces. These results demonstrate how affinity-altering changes in intersubunit interactions can be produced by mutations at structurally remote sites. |
| Document Type: |
article |
| File Description: |
electronic resource |
| Language: |
English |
| ISSN: |
1932-6203 |
| Relation: |
http://europepmc.org/articles/PMC5376325?pdf=render; https://doaj.org/toc/1932-6203 |
| DOI: |
10.1371/journal.pone.0174921 |
| Access URL: |
https://doaj.org/article/ddcbca32f25844b3a2789a4c6a2341e3 |
| Accession Number: |
edsdoj.bca32f25844b3a2789a4c6a2341e3 |
| Database: |
Directory of Open Access Journals |
