6HBW

Crystal structure of deoxy-human hemoglobin beta6 glu->trp

6HBW の概要

• エントリーDOI: 10.2210/pdb6hbw/pdb
• 分子名称: PROTEIN (HEMOGLOBIN ALPHA 1), PROTEIN (HEMOGLOBIN BETA), PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• 機能のキーワード: oxygen transport, hemoglobin, oxygen storage-transport complex, oxygen storage/transport
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 64661.25

構造登録者

Harrington, D.J.,Adachi, K.,Royer Jr., W.E. (登録日: 1998-09-10, 公開日: 1998-09-16, 最終更新日: 2023-09-20)

主引用文献

Harrington, D.J.,Adachi, K.,Royer Jr., W.E.
Crystal structure of deoxy-human hemoglobin beta6 Glu --> Trp. Implications for the structure and formation of the sickle cell fiber.
J.Biol.Chem., 273:32690-32696, 1998

PubMed Abstract: An atomic-level understanding of the interactions between hemoglobin molecules that contribute to the formation of pathological fibers in sickle cell disease remains elusive. By exploring crystal structures of mutant hemoglobins with altered polymerization properties, insight can be gained into sickle cell hemoglobin (HbS) polymerization. We present here the 2.0-A resolution deoxy crystal structure of human hemoglobin mutated to tryptophan at the beta6 position, the site of the glutamate --> valine mutation in HbS. Unlike leucine and isoleucine, which promote polymerization relative to HbS, tryptophan inhibits polymerization. Our results provide explanations for the altered polymerization properties and reveal a fundamentally different double strand that may provide a model for interactions within a fiber and/or interactions leading to heterogeneous nucleation.

PubMed: 9830011
DOI: 10.1074/jbc.273.49.32690

実験手法

X-RAY DIFFRACTION (2 Å)