Structural Studies of SARS Virus Nsp15 and Human Innate Immunity Receptor TLR3 | 2D Crystallization and 3D Reconstruction of Biological Macromolecules: A Promising Approach for Molecular Structural Biology and Nanotechnology

Jing-chuan Sun

ISBN 10: 3639063104 / ISBN 13: 9783639063103

Published by VDM Verlag Dr. Müller, 2008

About this Item

Structural Studies of SARS Virus Nsp15 and Human Innate Immunity Receptor TLR3 | 2D Crystallization and 3D Reconstruction of Biological Macromolecules: A Promising Approach for Molecular Structural Biology and Nanotechnology | Jing-chuan Sun | Taschenbuch | Englisch | VDM Verlag Dr. Müller | EAN 9783639063103 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu.

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Bibliographic Details

• Title: Structural Studies of SARS Virus Nsp15 and Human Innate Immunity Receptor TLR3 | 2D Crystallization and 3D Reconstruction of Biological Macromolecules: A Promising Approach for Molecular Structural Biology and Nanotechnology
• Publisher: VDM Verlag Dr. Müller
• Publication Date: 2008
• Language: English
• ISBN 10: 3639063104
• ISBN 13: 9783639063103
• Binding: Taschenbuch
• Condition: Neu
• Dimensions: 8W x 150H x 220D millimeters 8 millimeters width by 150 millimeters height by 220 millimeters depth
• Weight: 213 grams
• Seller catalogs:
  • Bücher

About this title

Synopsis

3D structural determination of biological macromolecules is not only critical to understanding their mechanisms, but also essential in structural based drug discovery. Combining the high resolution imaging of TEM and efficient computer processing, protein structures in solution or in 2D crystals can be determined. Using lipid monolayer technique with Ni-NTA modified lipid, which has high affinity to 6His-tagged proteins, 2D crystal of the protein can be formed at the lipid surface. In this study, several proteins have been crystallized using this technique, including the SARS virus Nsp15 endonuclease and the human Toll-like receptor 3 extracellular domain. This approach may also have application in nanofabrication, taking advantage of the natural building bloc of proteins and virus. Single particle analysis can determine protein structures in solution without the need for crystals. 3D structures of several protein complexes had been solved by the single particle method, including IniA from Mycobacterium tuberculosis, Nsp15 and TLR3 ECD. Determining the structures of these proteins is an important step toward understanding pathogenic microbes and our immune system.

About the Author

Dr. Jingchuan Sun got his Ph.D at Texas A&M University and is now working at Brookhaven National Laboratory. He has many years' experience on 2D crystallization and TEM 3D reconstruction, and have succeeded on more than 10 proteins and virus. He has more than 10 publications on PNAS, JMB, JBC, etc.