Cell Recognition Proteins

CELL RECOGNITION PROTEINS 4

CellRecognition Proteins

Cellrecognition, also called cellularrecognition, describes the interaction between cells. In proteins,the interaction takes place on the membraneglycoproteins or surface molecules. It helps the cells to recognizetheir immediate environment. It is also regarded as the processthrough which the cells communicate to one another. Some of theexamples include Integrin (LFA-1) of T cell interacting with ICAM ofendothelial cell and Selectin (L) of lymphocyte interacting withaddressin (CD34) of endothelial cell. The recognition protein isfound the class of glycoproteins that are found above the plasmamembrane. The plasma membrane offers protection to the cell as wellas gives it shape. It also regulates the movement of substances intoand out of the cell. It can identify a cell as self or non-self.Glycoproteins are mainly attached to the polypeptides. They areessential integralmembrane proteins in enhancing the cell-cell interactions within abody. Glycoproteinsare important in enhancing the white blood cell recognition inmammals. Glycoproteinsare different amongst individuals hence making it difficult toundertake organ transplants. When it takes place, the white bloodcells assail the foreign MHC glycoproteins since they are obligatedto enhance immunity. TheCellRecognition Proteinsfunction as identification tags that aids in the detection of thecells to the immune system within a body (Kleanthous, 2000).

Glycoproteinsare also known to have the recognition sites. Ideally, these proteinshave sugar attachments. The recognition sites are found in the outersurface of the cell. Also known as the cell identity markers, theyare different from the receptor sites. They are to detect the foreigncells hence offer protection to the body. It is for this reason thatthe WBC destroys the bacteria that come into contact with the body.They also destroy foreign human cells. Topof Form

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Theshape of protein is essential as the substance is necessary tosupport life and it depends on the hydrogen bonding (Kleanthous,2000).The sequence in the amino acid identifies the shape of the protein.The shape of a protein defines its function in the bio-chemical orchemical process. Elongatedproteins are detached through mutual attraction by peptide chains(Atassi, 1987). Thespot has functional groups and formation that allows the molecules tojoin. Attractionenables the cells to hold onto other substances easily making itstraightforward to get elements from wide-range of substances. Withthe recognition proteins, the body cells can easily protectthemselves from foreign materials or organisms that cause ailments(Kleanthous, 2000).

Commonprotein-protein recognition is the receptor-ligand interaction. It isa process where a living cell gets external signals that enables itadjusts to a new environment using the surface receptors. Therecognition process has distinct characteristics namely multivalent,avidity-driven, and reversible (Kleanthous, 2000). As such, theresemblance among the contacting pair is low hence making itsusceptible to viruses. The viruses attack such a cell by generatinga stronger binding ability compared to the one linked to thephysiological ligands (Atassi, 1987). Anumber of interactions take place when the substrate molecule isbinding with the active site. Electrostatic interactions, hydrogenbonding and hydrophobic are some of the interactions that take place.In hydrophobic interactions, for instance, protein molecules repelwater molecules. Cell recognition proteins have important function tothe body including protection against foreign materials andcommunication between cells.

References

Atassi,M. Z. (1987). Immunobiologyof Proteins and Peptides IV: T-Cell Recognition and AntigenPresentation.Boston, MA: Springer US.

Kleanthous,C. (2000). Protein-proteinrecognition.Oxford [u.a.: Oxford Univ. Press.