STRUCTURE OF PENTAMERIC HUMAN SERUM AMYLOID-P COMPONENT

被引：416

作者：

EMSLEY, J

WHITE, HE

OHARA, BP

OLIVA, G

SRINIVASAN, N

TICKLE, IJ

BLUNDELL, TL

PEPYS, MB

WOOD, SP

机构：

[1] UNIV LONDON BIRKBECK COLL,MOLEC BIOL LAB,LONDON WC1E 7HX,ENGLAND

[2] UNIV LONDON BIRKBECK COLL,DEPT CRYSTALLOG,ICRF,STRUCT MOLEC BIOL UNIT,LONDON WC1E 7HX,ENGLAND

[3] HAMMERSMITH HOSP,ROYAL POSTGRAD MED SCH,IMMUNOL MED UNIT,LONDON W12 0NN,ENGLAND

来源：

NATURE | 1994年 / 367卷 / 6461期

关键词：

D O I：

10.1038/367338a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The three-dimensional structure of pentameric human serum amyloid P component at high resolution, the first reported for a pentraxin, reveals that the tertiary fold is remarkably similar to that of the legume lectins. Carboxylate and phosphate compounds bind directly to two calcium ions; interactions with a carboxyethylidene ring are mediated by Asn 59 and Gln 148 ligands of the calcium ions. These X-ray results indicate the probable modes of binding of the biologically important ligands, DNA and amyloid fibrils.

引用

页码：338 / 345

页数：8

共 42 条

[1]

AGRAWAL A, 1992, J BIOL CHEM, V267, P25352

[2] AMYLOID-P COMPONENT IS LOCATED ON ELASTIC FIBER MICROFIBRILS IN NORMAL HUMAN-TISSUE [J].