Sandbox Reserved 1658

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<p align="justify">Neuropilin is a transmembrane protein which has been highly conserved through evolution. Two different types of Neuropilin have been discovered in vertebrates: Neuropilin 1 (NRP1) and Neuropilin 2 (NRP2). They have 44% of similarity by comparing their amino acid sequences. In the human genome, it is located on the chromosome 10 and their molar weights flucatuate between 120 and 130 kDa.
<p align="justify">Neuropilin is a transmembrane protein which has been highly conserved through evolution. Two different types of Neuropilin have been discovered in vertebrates: Neuropilin 1 (NRP1) and Neuropilin 2 (NRP2). They have 44% of similarity by comparing their amino acid sequences. In the human genome, it is located on the chromosome 10 and their molar weights flucatuate between 120 and 130 kDa.
These proteins are particularly found in the membrane of the endothelial cells but the Neuropilin 1 is involved in several process such as axon guidance during the embryonic development, recognition of the Vascular Endothelial cell Growth Factor ([[VEGF]]) and recognition of covid-19.</p>
These proteins are particularly found in the membrane of the endothelial cells but the Neuropilin 1 is involved in several process such as axon guidance during the embryonic development, recognition of the Vascular Endothelial cell Growth Factor ([[VEGF]]) and recognition of covid-19.</p>
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<p align="justify"> The semaphorins (SEMA) bind to the (a1/a2/b1) domains while Vascular endothelial growth factors (VEGFs) bind to (b1/b2). The c domain as well as the transmembrane domain, are involved in the receptor dimerization.</p>
== Structural highlights ==
== Structural highlights ==

Revision as of 11:35, 9 January 2021

This Sandbox is Reserved from 26/11/2020, through 26/11/2021 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1643 through Sandbox Reserved 1664.
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extracellular domain of the Neuropilin 1

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