Hyper-Structured Molecules III


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Hongming Wang from Zhengzhou University, Prof.

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Wenjian Liu from Peking University for their kind suggestions and great help in the computational analysis about the possible structure of the molecule M2. Use the link below to share a full-text version of this article with your friends and colleagues. Learn more.

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Advanced Functional Materials Volume 18, Issue 2. China Search for more papers by this author. Cao E-mail address: caoshaokui zzu.

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Tools Request permission Export citation Add to favorites Track citation. Share Give access Share full text access. Share full text access. Please review our Terms and Conditions of Use and check box below to share full-text version of article. Citing Literature. The FR regions form a beta-sheet structure which serves as a scaffold to hold the HV regions in position to contact antigen.

1INTRODUCTION

This image represents the structure of an antibody's variable region Fab complexed with an antigen, in this case hen egg white lysozyme. The other images in this section are derived from this structure.


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The HV regions of a Fab, representing both light and heavy chains, are highlighted in purple. The antigen is green. The part of the antigen in direct contact with the antibody is called the antigenic determinant, or epitope.

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In this view, the HV regions of the Fab have been deleted. The FR regions of the antibody do not contact the antigen. This ribbon structure shows the antibody's HV purple and FR yellow regions of the Fab, and their interaction with an epitope of the antigen. Animation: FR and HV regions of antibody.

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Animation: Antigen interacts with HV region. An antigenic determinant, a site on the antigen that the immune system responds to by making antibody, can frequently be one unique structure on the antigen. In hen egg white lysozyme, a glutamine at position Gln protrudes away from the antigen surface. In this view, Gln is circled. The antibody is not shown. The following images show how this feature is important for the formation of a high affinity antibody-antigen interactions.


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The antibody's HV region forms an opening to surround the antigen's protruding Gln green. Hydrogen bonds yellow stabilize the antibody-antigen interaction. In addition to hydrogen bonds, other weak interactions such as van der Waals forces, hydrophobic interactions and electrostatic forces improve the binding specificity between antibody and antigen.

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Hyper-Structured Molecules III Hyper-Structured Molecules III
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