Src protein domain

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Src protein domain

Src protein domain. Computer model showing the primary (rods) and secondary (alpha helix, blue and beta sheets, purple) structures of the Src homology domain 3 (SH3). This protein domain binds ligands rich in the amino acid proline. It is found in many cytoplasmic proteins, including those that participate in signal transduction pathways

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Media ID 6274637

© LAGUNA DESIGN/SCIENCE PHOTO LIBRARY

Alpha Helix Beta Sheet Compound Compounds Computer Model Domain Molecules Primary Proteins Rods Secondary Sheets Signal Transduction Tyrosine Kinase Bio Chemistry Biochemical Computer Artwork Molecular Molecular Model Protein

EDITORS COMMENTS
This print from Science Photo Library showcases the intricate structure of the Src protein domain. The computer model beautifully depicts both the primary and secondary structures of this domain, with its rod-like shape representing the primary structure and the blue alpha helix and purple beta sheets symbolizing the secondary structures. The Src homology domain 3 (SH3) is a crucial binding domain that has an affinity for ligands abundant in proline amino acids. This versatile protein domain can be found in various cytoplasmic proteins involved in signal transduction pathways, playing a pivotal role in cellular communication. Through this stunning illustration, we gain insight into the complex world of biochemistry and molecular biology. The single molecule depicted here represents a fundamental building block within living organisms, highlighting its importance to biological processes. With its combination of scientific accuracy and artistic flair, this computer artwork provides us with a visual representation of how molecules like proteins are structured at their most basic level. It serves as a reminder that even seemingly simple compounds hold immense significance within our bodies. Science Photo Library continues to amaze us with their ability to capture these intricate details through their photographic expertise. This image stands as a testament to their commitment to showcasing cutting-edge scientific research without any commercial intentions.

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