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1XZ2

wild-type hemoglobin deoxy no-salt

1XZ2 の概要
エントリーDOI10.2210/pdb1xz2/pdb
関連するPDBエントリー1RQ3 1XYE 1XZ4
分子名称Hemoglobin alpha chain, Hemoglobin beta chain, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
機能のキーワードhemoglobin, globin, transport protein
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64547.05
構造登録者
主引用文献Kavanaugh, J.S.,Rogers, P.H.,Arnone, A.,Hui, H.L.,Wierzba, A.,Deyoung, A.,Kwiatkowski, L.D.,Noble, R.W.,Juszczak, L.J.,Peterson, E.S.,Friedman, J.M.
Intersubunit interactions associated with tyr42alpha stabilize the quaternary-T tetramer but are not major quaternary constraints in deoxyhemoglobin
Biochemistry, 44:3806-3820, 2005
Cited by
PubMed Abstract: Previous mutational studies on Tyr42alpha variants as well as the current studies on the mutant hemoglobin alphaY42A show that the intersubunit interactions associated with Tyr42alpha significantly stabilize the alpha1beta2 interface of the quaternary-T deoxyhemoglobin tetramer. However, crystallographic studies, UV and visible resonance Raman spectroscopy, CO combination kinetic measurements, and oxygen binding measurements on alphaY42A show that the intersubunit interactions formed by Tyr42alpha have only a modest influence on the structural properties and ligand affinity of the deoxyhemoglobin tetramer. Therefore, the alpha1beta2 interface interactions associated with Tyr42alpha do not contribute significantly to the quaternary constraints that are responsible for the low oxygen affinity of deoxyhemoglobin. The slight increase in the ligand affinity of deoxy alphaY42A correlates with small, mutation-induced structural changes that perturb the environment of Trp37beta, a critical region of the quaternary-T alpha1beta2 interface that has been shown to be the major source of quaternary constraint in deoxyhemoglobin.
PubMed: 15751957
DOI: 10.1021/bi0484670
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.9 Å)
構造検証レポート
Validation report summary of 1xz2
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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