7AAE

Crystal structure of Human serum albumin in complex with myristic acid at 2.27 Angstrom Resolution

これはPDB形式変換不可エントリーです。

7AAE の概要

• エントリーDOI: 10.2210/pdb7aae/pdb
• 分子名称: Albumin, MYRISTIC ACID, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (6 entities in total)
• 機能のキーワード: serum protein, lipid binding protein, drug carrier, protein transport
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 68558.22

構造登録者

Maso, L.,Liberi, S.,Trande, M.,Angelini, A.,Cendron, L. (登録日: 2020-09-04, 公開日: 2021-02-24, 最終更新日: 2024-11-06)

主引用文献

Maso, L.,Trande, M.,Liberi, S.,Moro, G.,Daems, E.,Linciano, S.,Sobott, F.,Covaceuszach, S.,Cassetta, A.,Fasolato, S.,Moretto, L.M.,De Wael, K.,Cendron, L.,Angelini, A.
Unveiling the binding mode of perfluorooctanoic acid to human serum albumin.
Protein Sci., 30:830-841, 2021

PubMed Abstract: Perfluorooctanoic acid (PFOA) is a toxic compound that is absorbed and distributed throughout the body by noncovalent binding to serum proteins such as human serum albumin (hSA). Though the interaction between PFOA and hSA has been already assessed using various analytical techniques, a high resolution and detailed analysis of the binding mode is still lacking. We report here the crystal structure of hSA in complex with PFOA and a medium-chain saturated fatty acid (FA). A total of eight distinct binding sites, four occupied by PFOAs and four by FAs, have been identified. In solution binding studies confirmed the 4:1 PFOA-hSA stoichiometry and revealed the presence of one high and three low affinity binding sites. Competition experiments with known hSA-binding drugs allowed locating the high affinity binding site in sub-domain IIIA. The elucidation of the molecular basis of the interaction between PFOA and hSA might provide not only a better assessment of the absorption and elimination mechanisms of these compounds in vivo but also have implications for the development of novel molecular receptors for diagnostic and biotechnological applications.

PubMed: 33550662
DOI: 10.1002/pro.4036

実験手法

X-RAY DIFFRACTION (2.27 Å)