1XZ2
wild-type hemoglobin deoxy no-salt
1XZ2 の概要
| エントリーDOI | 10.2210/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 | 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. (登録日: 2004-11-11, 公開日: 2004-11-30, 最終更新日: 2023-08-23) |
| 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: 15751957DOI: 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
検証レポート(詳細版)
をダウンロード






