Sh2 Domains
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Sh2 Domains
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Author : Kazuya Machida
language : en
Publisher: Humana
Release Date : 2018-06-09
Sh2 Domains written by Kazuya Machida and has been published by Humana this book supported file pdf, txt, epub, kindle and other format this book has been release on 2018-06-09 with Science categories.
This volume covers an array of techniques available for studying SH2 domains and phosphotyrosine signaling. The book is divided into six parts: Part I outlines the history of SH2, technology development, and cell signaling; Part II focuses on computational approaches and tools used for identification, classification, and predictions of SH2 domain binding partners; Part III details various ways to prepare the SH2 domains as experimental reagents; Part IV presents methods for structural analysis and conventional binding assays using SH2 domains; Part V describes high-throughput and proteomics approaches to aid in analyzing SH2-mediated interactions; and Part VI covers applications for SH2 domain to functional and imaging analyzes. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Cutting-edge and thorough, SH2 Domains: Methods and Protocols is a valuable resource for computational biologists, biochemists, structural biologists, cell biologists, pathologists, and people interested in SH2 domains and phosphotyrosine signaling. Researchers who are investigating how protein interaction domain mediate specificity in signaling systems may also find this book informative.
Sh2 Domains
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Author : Teresa Carlomagno
language : en
Publisher: Springer Nature
Release Date : 2023-09-05
Sh2 Domains written by Teresa Carlomagno and has been published by Springer Nature this book supported file pdf, txt, epub, kindle and other format this book has been release on 2023-09-05 with Science categories.
This volume looks at the latest methods used to study and modulate the biological function and mechanisms of SH2 domains. The chapters in this book are organized into five parts. Part One presents methodology aimed at determining the structures and dynamics of SH2 domains and their complexes with phosphopeptides. Part Two discusses techniques to understand and predict interactions of SH2 domains by measuring or calculating their affinity to phosphopeptides. Part Three focuses on inhibitors of SH2 domains that lead the way for chemical tool development and drug discovery. Part Four describes how to evolve and engineer SH2 domains with specific binding properties, and Part Five explores how to measure the regulation of protein tyrosine phosphatase activity through allosteric binding of peptides to SH2 domains and condensation. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Cutting-edge and comprehensive, SH2 Domains: Functional Modules and Evolving Tools in Biology is a valuable resource for researchers, working in the biophysical and biochemical field, who want to learn more about this exciting and versatile class of regulatory and signaling domains.
Binding Specificity Of Sh2 Domains Revealed By A Combinatorial Peptide Library
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Author : Andrew Kunys
language : en
Publisher:
Release Date : 2013
Binding Specificity Of Sh2 Domains Revealed By A Combinatorial Peptide Library written by Andrew Kunys and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2013 with categories.
Abstract: Src homology 2 Domains (SH2 domains) are modular protein binding domains which recognize a phosphotyrosine and the residues adjacent to the phosphotyrosine. Although they are known to bind to specific phosphopeptides motifs, the exact peptide binding motifs for each of the 120 human SH2 domains are not known. These proteins are associated mainly with cellular signaling affecting processes as disparate as apoptosis and proliferation. In this work, high quality specificity data was obtained from 18 different SH2 domains by screening them individually against a One-Bead-One-Peptide library. Interestingly, no two domains have the same specificity, suggesting that subtle differences mark each domain as unique. Further, most of the domains studied recognize multiple different classes of binding peptides, which implies their role in binding may be more complicated that previously realized. The data obtained is unique, in that no other method can produce data of high enough quality to unambiguously establish the subtle specificity patterns of each domain or decipher the data obtained from a domain which can recognize multiple peptide ligand classes. This data will provide insight into the basic biology of cell signaling and should prove to be a valuable resource to researchers studying in this area.
Sh Domains
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Author : Natalya Kurochkina
language : en
Publisher: Springer
Release Date : 2015-07-17
Sh Domains written by Natalya Kurochkina and has been published by Springer this book supported file pdf, txt, epub, kindle and other format this book has been release on 2015-07-17 with Science categories.
This book covers structure, function, and important roles of the SH domains, structure-function relationships, the versatile nature of their action, mechanisms of aggregation, specificity of interactions, impact of mutations on protein functional dysregulation, and cell signaling. Their involvement in various cellular processes such as migration, invasiveness, actin reorganization, shaping spines, determination of the morphology assembly of fibrils, and mechanotransduction makes these molecules attractive drug targets. Substrates, inhibitors and activators of PTKs present a wide variety of therapeutic agents in the context of delivering treatments for numerous pathologies. The new emerging field of stem cell therapies and design of biomaterials for treatments relies on the directed regulation of stem cell growth, differentiation and morphology, as well as the production of biomimetic scaffolds that respond to programmed signals. Advances in deciphering the mechanisms of action of these important molecules will lead to the implementation and success of their vital applications.
Selectivity And Structure Of Chimeric Loop Swaps In Sh2 Domains
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Author : Sarah N. Smith
language : en
Publisher:
Release Date : 2023
Selectivity And Structure Of Chimeric Loop Swaps In Sh2 Domains written by Sarah N. Smith and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2023 with Chemical structure categories.
SH2 (Src Homology 2) domains are protein domains that bind to phosphorylated tyrosine residues within cell signaling cascades. They have been found to play a role in certain cancers and immunological disorders. Despite their importance in cell signaling and medical relevance, the structural basis of the various selectivity classes of SH2 domains is only partially understood. Previous research found that the EF and BG loops of the domains contribute to forming the peptide binding pocket, and thus impact their selectivity. To further understand the role of these loops in selectivity, we engineered chimeric SH2 domains by swapping the EF and BG loops from other SH2 domains into the backbone of c-Src SH2. Methods of fluorescence polarization, Ki binding assays, computer modeling, and X-ray crystallography were used to test if the loops can alter selectivity and structure. We found that the chimeras had a lower affinity for the *pYEEI (pY refers to phosphorylated tyrosine) peptide than the wild-type Src-SH2 domain, showing the loop swap alters the disassociation constant of the chimeras for this target peptide. Broad variability was also observed through Ki competition assays. The structures of several chimeras were also visualized through computational molecular modeling, suggesting alterations in the structure of the binding pocket. These results provide further evidence for these loops contributing to the selectivity of SH2 domains, and a better understanding of how these domains function.
Solution Structure And Electrostatic Properties Of An Sh2 Domain Phosphopeptide Complex
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Author : Alex Uriel Singer
language : en
Publisher:
Release Date : 1998
Solution Structure And Electrostatic Properties Of An Sh2 Domain Phosphopeptide Complex written by Alex Uriel Singer and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 1998 with categories.
Specificity Of Sh2 Domains And Protein Tyrosine Phosphatases
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Author :
language : en
Publisher:
Release Date : 1997
Specificity Of Sh2 Domains And Protein Tyrosine Phosphatases written by and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 1997 with categories.
Stucture Function Study Of Sh2 Domains
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Author : Luc Edgar Micheline Marengére
language : en
Publisher:
Release Date : 1994
Stucture Function Study Of Sh2 Domains written by Luc Edgar Micheline Marengére and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 1994 with categories.
Biophysical Characterisation Of Sh2 Domains
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Author :
language : en
Publisher:
Release Date : 2009
Biophysical Characterisation Of Sh2 Domains written by and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2009 with categories.
Modular Protein Domains
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Author : Giovanni Cesareni
language : en
Publisher: John Wiley & Sons
Release Date : 2006-03-06
Modular Protein Domains written by Giovanni Cesareni and has been published by John Wiley & Sons this book supported file pdf, txt, epub, kindle and other format this book has been release on 2006-03-06 with Science categories.
Since the full functionality of any given protein can only be understood in terms of its interaction with other, often regulatory proteins, this unique reference source covers all relevant protein domains, including SH2, SH3, PDZ, WW, PTB, EH, PH and PX. Its user-oriented concept combines broad coverage with easy retrieval of essential information, and includes a special section on Web-based tools and databases covering protein modules and functional peptide motifs. Essential for the study of protein-protein interactions in vivo or in silico, and a prerequisite for successful functional proteomics studies. With a prologue by Sir Tom Blundell.