STRUCTURE OF THE CRYSTALLINE COMPLEX OF CYTIDYLIC ACID (2'-CMP) WITH RIBONUCLEASE AT 1.6 ANGSTROM RESOLUTION - CONSERVATION OF SOLVENT SITES IN RNASE-A HIGH-RESOLUTION STRUCTURES

被引：41

作者：

LISGARTEN, JN

GUPTA, V

MAES, D

WYNS, L

ZEGERS, I

PALMER, RA

DEALWIS, CG

AGUILAR, CF

HEMMINGS, AM

机构：

[1] UNIV LONDON BIRKBECK COLL,DEPT CRYSTALLOG,LONDON WC1E 7HX,ENGLAND

[2] VRIJE UNIV BRUSSELS,INST MOLEK BIOL,DEPT ULTRASTRUCT,B-1640 RHODE ST GENESE,BELGIUM

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1993年 / 49卷

关键词：

D O I：

10.1107/S090744499300719X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The X-ray structure of the inhibitor complex of bovine ribonuclease A with cytidylic acid (2'-CMP) has been determined at 1.6 Angstrom resolution and refined by restrained least squares to R = 0.17 for 11 945 reflections. Binding of the inhibitor molecule to the protein is confirmed to be in the productive mode associated with enzyme activity. Q study of conserved solvent sites amongst high-resolution structures in the same crystal form reveals a stabilizing water cluster between the N and C termini.

引用

页码：541 / 547

页数：7

共 31 条

[1] NEWLY OBSERVED BINDING MODE IN PANCREATIC RIBONUCLEASE [J].