NMR docking of a substrate into the X-ray structure of staphylococcal nuclease-Reference-Cited by-同舟云学术

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NMR docking of a substrate into the X-ray structure of staphylococcal nuclease

Published:1992-08 Issue:4 Volume:13 Page:275-287
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Genetics
language:en
Short-container-title:Proteins

Author:

Weber David J.,Gittis Apostolos G.,Mullen Gregory P.,Abeygunawardana Chitrananda,Lattman Eaton E.,Mildvan Albert S.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Reference44 articles.

1. Staphylococcal nuclease reviewed: A prototypic study in contemporary enzymology

2. Staphylococcal nuclease: Proposed mechanism of action based on structure of enzyme--thymidine 3',5'-bisphosphate--calcium ion complex at 1.5-A resolution

3. The crystal structure of the ternary complex of staphylococcal nuclease, Ca2+ and the inhibitor pdTp, refined at 1.65 Å

4. Staphylococcal nuclease: sequential assignments and solution structure

5. Two-dimensional NMR studies of Staphylococcal nuclease. 1. Sequence-specific assignments of hydrogen-1 signals and solution structure of the nuclease H124L-thymidine 3',5'-bisphosphate-calcium ternary complex

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