Uncapping the N-terminus of a ubiquitous His-tag peptide enhances its Cu2+ binding affinity

被引：8

作者：

Watly, J. ^{[1
]}

Hecel, A. ^{[1
]}

Wieczorek, R. ^{[1
]}

Swiatek-Korlowska, J. ^{[2
]}

Kozlowski, H. ^{[1
,2
]}

Rowinska-Zyrek, M. ^{[1
]}

机构：

[1] Univ Wroclaw, Fac Chem, F Joliot Curie 14, PL-50383 Wroclaw, Poland

[2] Publ Higher Med Profess Sch Opole, Katowicka 68, PL-45060 Opole, Poland

来源：

DALTON TRANSACTIONS | 2019年 / 48卷 / 36期

关键词：

SNAKE-VENOM METALLOPROTEINASES; COPPER(II); HISTIDINE; FAMILY; IONS; COORDINATION; COMPLEXES; CU(II); EQUILIBRIA; CONSTANTS;

D O I：

10.1039/c9dt01635j

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

Metal complexes with an N-terminally free and N-terminally acetylated polyhistidine region of Echis ocellatus venom, with an interesting His-rich motif present in numerous metal binding proteins from all kingdoms of life (DHDHDHHHHHHPGSSV-NH2 and Ac-DHDHDHHHHHHPGSSV-NH2) show the role of the free amino group in the thermodynamic enhancement of Cu2+, Ni2+ and Zn2+ binding. In the studied sequences, Cu2+ can be coordinated by different sets of imidazole rings, and a 3-10 helix is detected in close proximity of Cu2+ binding sites. The complexes are more stable than those with a typical His6-tag, despite a similar copper(II) coordination mode in both cases.

引用

页码：13567 / 13579

页数：13

共 22 条

[21] Structural model of a2-subunit N-terminus and its binding interface for Arf-GEF CTH2: Implication for regulation of V-ATPase, CTH2 function and rational drug design
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[22] STRUCTURE-FUNCTION-RELATIONSHIPS OF THE HUMAN IL-8 RECEPTORS .1. ROLE OF THE N-TERMINUS IN DETERMINING SUBTYPE SELECTIVITY .2. MAPPING OF DISTINCT HIGH AND LOW-AFFINITY BINDING-SITES THAT MEDIATE IL8RB ACTIVATION
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