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PMID: 7664036 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Comparison of four independently determined structures of human recombinant interleukin-4.

Nature structural biology ·Vol. 1 ·No. 5 ·1994-05-00 ·Pages 301-10

Smith LJ, Redfield C, Smith RA, Dobson CM, Clore GM, Gronenborn AM, Walter MR, Naganbushan TL, Wlodawer A

Abstract

Four independent structures of human interleukin-4, two determined by nuclear magnetic resonance techniques and two by X-ray diffraction, have been compared in detail. The core of this four helix bundle protein is very similar in all the structures but there are some differences in loop regions that are known to be mobile in solution. Careful comparison of the experimental data sets and the methods of analysis of the different laboratories has provided clues to the sources of most of the differences, and also answered some general questions about the accuracy of protein structure determination by these two techniques.

MeSH Terms
Crystallography, X-Ray Humans Interleukin-4/chemistry Magnetic Resonance Spectroscopy Models, Molecular Protein Conformation Recombinant Fusion Proteins/chemistry
Chemicals
Recombinant Fusion Proteins Interleukin-4
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Smith L J
Oxford Centre for Molecular Sciences, University of Oxford, UK.
Redfield C
Smith R A
Dobson C M
Clore G M
Gronenborn A M
Walter M R
Naganbushan T L
Wlodawer A
Article Info
Journal
Nature structural biology
Abbr.
Nat Struct Biol
ISSN
1072-8368
Published
1994-05-00
Pages
301-10
Language
English
Region
United States
NLM ID
9421566
Subset
IM
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