3-DIMENSIONAL STRUCTURE OF HUMAN [(CD7)-CD-113]METALLOTHIONEIN-2 IN SOLUTION DETERMINED BY NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY

被引：153

作者：

MESSERLE, BA ^{[1
]}

SCHAFFER, A ^{[1
]}

VASAK, M ^{[1
]}

KAGI, JHR ^{[1
]}

WUTHRICH, K ^{[1
]}

机构：

[1] UNIV ZURICH,INST BIOCHEM,CH-8057 ZURICH,SWITZERLAND

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1990年 / 214卷 / 03期

关键词：

D O I：

10.1016/0022-2836(90)90291-S

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：

The three-dimensional structure of human [113Cd7]metallothionein-2 was determined by nuclear magnetic resonance spectroscopy in solution. Sequence-specific 1H resonance assignments were obtained using the sequential assignment method. The input for the structure calculations consisted of the metal-cysteine co-ordinative bonds identified with heteronuclear correlation spectroscopy, 1H-1H distance constraints from nuclear Overhauser enhancement spectroscopy, and spin-spin coupling constants 3JHNαand3Jαβ. The molecule consists of two domains, the β-domain including amino acid residues 1 to 30 and three metal ions, and the α-domain including residues 31 to 61 and four metal ions. The nuclear magnetic resonance data present no evidence for a preferred relative orientation of the two domains. The polypeptide-to-metal co-ordinative bonds in human metallothionein-2 are identical to those in the previously determined solution structures of rat metallothionein-2 and rabbit metallothionein-2a, and the polypeptide conformations in the three proteins are also closely similar. © 1990.

引用

页码：765 / 779

页数：15

共 43 条

[31] TWO-DIMENSIONAL DOUBLE QUANTUM H-1-NMR SPECTROSCOPY OF PROTEINS [J].