Transmembrane protease serine 2
From Proteopedia
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TMPRSS2 is a membrane protein belonging to the '''type II transmembrane serine protease (TTSP) family'''. It is functionally classified as a '''trypsin-like protease''' (TLP). <ref>DOI 10.3389/fmolb.2021.666626</ref> Serine proteases are known to be involved in many physiological and pathological processes. | TMPRSS2 is a membrane protein belonging to the '''type II transmembrane serine protease (TTSP) family'''. It is functionally classified as a '''trypsin-like protease''' (TLP). <ref>DOI 10.3389/fmolb.2021.666626</ref> Serine proteases are known to be involved in many physiological and pathological processes. | ||
| + | |||
| + | == Protease activity == | ||
== General function == | == General function == | ||
In terms of normal function, TMPRSS2 has | In terms of normal function, TMPRSS2 has | ||
| - | been associated with physiological and | + | been associated with physiological and pathological processes such as digestion, tissue remodelling, blood coagulation, fertility, inflammatory |
responses, tumour cell invasion, apoptosis and | responses, tumour cell invasion, apoptosis and | ||
pain. <ref>DOI 10.1097/j.pain.0000000000000130</ref> | pain. <ref>DOI 10.1097/j.pain.0000000000000130</ref> | ||
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
| - | == | + | == Structure == |
| - | == | + | == Expression == |
| - | == | + | == Phamcacological therapeutic approaches == |
== Structural highlights == | == Structural highlights == | ||
Revision as of 15:45, 28 November 2021
TMPRSS2 is a membrane protein belonging to the type II transmembrane serine protease (TTSP) family. It is functionally classified as a trypsin-like protease (TLP). [1] Serine proteases are known to be involved in many physiological and pathological processes.
Protease activity
General function
In terms of normal function, TMPRSS2 has been associated with physiological and pathological processes such as digestion, tissue remodelling, blood coagulation, fertility, inflammatory responses, tumour cell invasion, apoptosis and pain. [2]
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References
- ↑ Sgrignani J, Cavalli A. Computational Identification of a Putative Allosteric Binding Pocket in TMPRSS2. Front Mol Biosci. 2021 Apr 30;8:666626. doi: 10.3389/fmolb.2021.666626., eCollection 2021. PMID:33996911 doi:http://dx.doi.org/10.3389/fmolb.2021.666626
- ↑ Lam DK, Dang D, Flynn AN, Hardt M, Schmidt BL. TMPRSS2, a novel membrane-anchored mediator in cancer pain. Pain. 2015 May;156(5):923-930. doi: 10.1097/j.pain.0000000000000130. PMID:25734995 doi:http://dx.doi.org/10.1097/j.pain.0000000000000130
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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Paula R. Mallavibarrena, Ines Muniesa-Martinez, Michal Harel, Laura Aleixos Juan, Jaime Prilusky
