Mass spectrometry-based footprinting of protein-protein interactions

被引：14

作者：

Mckee, Christopher J.

Kessl, Jacques J.

Norris, Jocelyn O.

Shkriabai, Nikolozi

Kvaratskhelia, Mamuka ^{[1
]}

机构：

[1] Ohio State Univ, Coll Pharm, Ctr Retrovirus Res, Columbus, OH 43210 USA

来源：

METHODS | 2009年 / 47卷 / 04期

关键词：

Protein-protein interactions; Mass spectrometric footprinting; Surface topology of proteins; Amino acid modifying reagents; MALDI-ToF; HUMAN-IMMUNODEFICIENCY-VIRUS; INTEGRASE-BINDING DOMAIN; VIRAL-DNA BINDING; HIV-1; INTEGRASE; ENZYMATIC-ACTIVITY; CRYSTAL-STRUCTURE; IN-VITRO; LEDGF/P75; REPLICATION; REVEALS;

D O I：

10.1016/j.ymeth.2008.10.023

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

We present a high-resolution mass spectrometric (MS) footprinting method enabling identification of contact amino acids in protein-protein complexes. The method is based on comparing surface topologies of a free protein versus its complex with the binding partner using differential accessibility of small chemical group selective modifying reagents. Subsequent MS analysis reveals the individual amino acids selectively shielded from modification in the protein-protein complex. The current report focuses on probing interactions between full-length HIV-1 integrase and its principal cellular partner lens epithelium-derived growth factor. This method has a generic application and is particularly attractive for studying large protein-protein interactions that are less amenable for crystallographic or NMR analysis. (C) 2008 Elsevier Inc. All rights reserved.

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收藏

页码：304 / 307

页数：4

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