Download Encyclopedia of Molecular Pharmacology 2 volume set by Stefan Offermanns, Walter Rosenthal PDF
By Stefan Offermanns, Walter Rosenthal
An crucial textual content, it is a absolutely up to date moment version of a vintage, now in volumes. It presents fast entry to details on molecular pharmacology for examine scientists, clinicians and complicated scholars. With the A-Z layout of over 2,000 entries, round 350 authors supply an entire connection with the realm of molecular pharmacology. The e-book combines the information of vintage pharmacology with the more moderen procedure of the best research of the molecular mechanisms wherein medicines exert their results. brief key-phrase entries outline universal acronyms, phrases and words. additionally, exact essays supply in-depth details on medications, mobile tactics, molecular ambitions, suggestions, molecular mechanisms, and basic principles.
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Sequestering Signaling Components Specificity in signal transduction is also achieved by selective separation of signaling components. By associating with specific proteins and bringing them together, adaptor proteins can determine how the pathway propagates through the cell. This is important for ▶Ras signaling, for example. Ras, which can be activated in response to large number of growth factors and signaling cues, regulates multiple pathways. Therefore, by sequestering specific proteins, adaptor proteins ensure that a particular stimulus activates the appropriate pathway(s).
15 Basic Mechanisms Adaptor proteins function by simultaneously interacting with multiple components of a signaling pathway (Fig. 2). In order to be able to bind to more than one target protein at the same time, adaptor proteins contain at least two specific protein-protein interaction domains. These domains recognize specific motifs in the target proteins and can act completely independently, like beads on a string, or interact with another domain within the same molecule. Such intramolecular interactions can regulate the ability of each domain to bind to its target.
Intramolecular Interactions Another way in which the function of adaptor proteins is regulated is through modulation of intramolecular interactions. Often one domain will bind to another domain in the same adaptor molecular, preventing further interactions with other proteins. An example of this is found in the adaptor protein, Crk. Crk contains an N-terminal SH2 domain, followed by two SH3 domains. The SH3 domains are separated by a linker region containing a tyrosine residue. When Crk is phosphorylated by a tyrosine kinase, such as Abl, the intrinsic SH2 domain binds to the phosphotyrosine, attenuating Crk signaling activity.