Musculoskeletal System
The musculoskeletal system, also called the locomotor system, is an organ system that gives humans and animals the ability to move using their muscular and skeletal systems. It provides stability, form, support, and movement to the body. The skeleton is composed of bones (skeleton), muscles, cartilage, tendons, ligaments, joints, and other connective tissue that supports and binds tissues and organs together. The musculoskeletal system is subdivided into two broad systems, such as the muscular system and the skeletal system.
Skeletal structure
The skeletal system is the core framework of the human body. The skeletal structure comprises bones and connective tissue, including cartilage, ligaments, and tendons. The skeletal structure of our body acts as a support structure. It maintains the body's shape and is responsible for its movement, blood cell formation, protection of organs, and mineral storage. The skeletal system is referred to as the musculoskeletal system.
Explain in detail the funcations and signalling of ephrin receptors.
Provide examples.
Eph receptors are a class of receptors that are activated in response to interaction with Eph receptor-interacting proteins (Ephs, after erythropoietin-producing human hepatocellular receptors) (Ephrins). The biggest known subfamily of receptor tyrosine kinases is made up of Ephs (RTKs). Eph receptor activation requires direct cell-cell contacts, and both Eph receptors and the associated ephrin ligands are membrane-bound proteins. Axon guidance, the creation of tissue borders, cell migration, and segmentation are just a few of the activities crucial to embryonic development that have been linked to eph/ephrin signaling.
Based on their sequence similarity and their affinity for either the transmembrane-bound ephrin-B ligands or the glycosylphosphatidylinositol-linked ephrin-A ligands, Ephs can be split into two subclasses, EphAs and EphBs (encoded by the chromosomal loci named EPHA and EPHB respectively). Nine EphAs (EphA1-8 and EphA10) and five EphBs are known to be expressed in humans out of the 16 Eph receptors (see above) that have been found in animals (EphB1-4 and EphB6). Ephs of a certain subclass typically attach to all ephrins of that subclass preferentially, with little to no cross-binding to ephrins of the opposing subclass. Recent research has suggested that the distinct binding strategies employed by EphAs and EphBs may be partially responsible for the intrasubclass specificity of Eph/ephrin binding.
Ephrin-B3 and ephrin-A5 have recently been demonstrated to bind to and activate EphA4 and EphB2, respectively, demonstrating that there are some exceptions to the intrasubclass binding specificity reported in Ephs. Ephrin-As bind via a "lock-and-key" mechanism that requires little conformational change of the EphAs, whereas EphBs use a "induced fit" mechanism that uses more energy to change the conformation of EphBs in order to bind to ephrin-Bs. EphA/ephrin-A interactions typically occur with higher affinity than EphB/ephrin-B interactions, which can be partially
There are 16 Ephs known to exist in animals, and they are as follows:
EPHA 1, EPHA 2, EPHA 3, EPHA 5, EPHA 6, EPHA 7, EPHA 8, EPHA 9, and EPHA 10
EPHB1, EPHB2, EPHB3, EPHB4, EPHB5, EPHB6
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