Chemical cross-linking and native mass spectrometry: A fruitful combination for structural biology

被引:102
作者
Sinz, Andrea [1 ]
Arlt, Christian [1 ]
Chorev, Dror [2 ]
Sharon, Michal [2 ]
机构
[1] Univ Halle Wittenberg, Inst Pharm, Dept Pharmaceut Chem & Bioanalyt, D-06120 Halle, Germany
[2] Weizmann Inst Sci, Dept Biol Chem, IL-76100 Rehovot, Israel
关键词
chemical cross-linking; native mass spectrometry; protein 3D structure; protein-protein interactions; PROTEIN-PROTEIN INTERACTIONS; SURFACE-INDUCED DISSOCIATION; GAS-PHASE; ELECTROSPRAY-IONIZATION; LINKED PEPTIDES; MACROMOLECULAR ASSEMBLIES; ESCHERICHIA-COLI; SOFTWARE TOOL; SUBUNIT ARCHITECTURE; REGULATORY PARTICLE;
D O I
10.1002/pro.2696
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Mass spectrometry (MS) is becoming increasingly popular in the field of structural biology for analyzing protein three-dimensional-structures and for mapping protein-protein interactions. In this review, the specific contributions of chemical crosslinking and native MS are outlined to reveal the structural features of proteins and protein assemblies. Both strategies are illustrated based on the examples of the tetrameric tumor suppressor protein p53 and multisubunit vinculin-Arp2/3 hybrid complexes. We describe the distinct advantages and limitations of each technique and highlight synergistic effects when both techniques are combined. Integrating both methods is especially useful for characterizing large protein assemblies and for capturing transient interactions. We also point out the future directions we foresee for a combination of in vivo crosslinking and native MS for structural investigation of intact protein assemblies.
引用
收藏
页码:1193 / 1209
页数:17
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