User:Ophelie Lefort/Sandbox
From Proteopedia
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The protein has a 283 amino-acids long sequence with two mainly domains. It forms a kind of elongate sphere of approximately 70Å large and 150Å long (dimensions: 70,37Å X 70,37Å X 105,02Å). The protein is composed of signal peptide (1-31) which leads to the location in azurophil granules [http://www.jimmunol.org/content/191/5/2700] and allows its excretion. In addition there is a protease domain (32-283) which is a trypsin-like domain with a trypsin-like active site, according to the specificity for P1-Arg residues, but this domain can be an elastase-like active site according to the primary sequence (because of the presence of a swallow S1 pocket) specific to small aliphatic residues. [http://www.cell.com/structure/fulltext/S0969-2126(14)00238-X] | The protein has a 283 amino-acids long sequence with two mainly domains. It forms a kind of elongate sphere of approximately 70Å large and 150Å long (dimensions: 70,37Å X 70,37Å X 105,02Å). The protein is composed of signal peptide (1-31) which leads to the location in azurophil granules [http://www.jimmunol.org/content/191/5/2700] and allows its excretion. In addition there is a protease domain (32-283) which is a trypsin-like domain with a trypsin-like active site, according to the specificity for P1-Arg residues, but this domain can be an elastase-like active site according to the primary sequence (because of the presence of a swallow S1 pocket) specific to small aliphatic residues. [http://www.cell.com/structure/fulltext/S0969-2126(14)00238-X] | ||
| - | The active is form by 4 amino acids: Gly(189), Phe(190, Ser(216), D(226)<ref>DOI: http://dx.doi.org/10.1016/j.str.2014.07.008<ref> | + | The active is form by 4 amino acids: Gly(189), Phe(190, Ser(216), D(226)<ref>NSP4 Is Stored in Azurophil Granules and Released by Activated Neutrophils as Active Endoprotease with Restricted Specificity |
| + | Natascha C. Perera, Karl-Heinz Wiesmüller, Maria Torp Larsen, Beate Schacher, Peter Eickholz, Niels Borregaard and Dieter E. Jenne DOI: http://dx.doi.org/10.1016/j.str.2014.07.008<ref> | ||
The residue F190 obstructs the active site which could normally not links a P1-Arg. However, a study[http://www.cell.com/structure/fulltext/S0969-2126(14)00238-X] considered the possibility that the two residues S216 and F190 of the active site can form a flexible gate which allows P1-Arg to enter. Then, the link between the active site and P1-Arg can be stabilized by a salt bridge interaction between S1-D226 and P1-Arg. | The residue F190 obstructs the active site which could normally not links a P1-Arg. However, a study[http://www.cell.com/structure/fulltext/S0969-2126(14)00238-X] considered the possibility that the two residues S216 and F190 of the active site can form a flexible gate which allows P1-Arg to enter. Then, the link between the active site and P1-Arg can be stabilized by a salt bridge interaction between S1-D226 and P1-Arg. | ||
The hypothesis of the flexible gate was confirmed by the same study. The mutations of S216 only, F190 only or both together show a forced full open gate is more efficient than a forced partially open gate. | The hypothesis of the flexible gate was confirmed by the same study. The mutations of S216 only, F190 only or both together show a forced full open gate is more efficient than a forced partially open gate. | ||
Revision as of 19:32, 25 January 2017
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References
- ↑ 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
- ↑ NSP4 Is Stored in Azurophil Granules and Released by Activated Neutrophils as Active Endoprotease with Restricted Specificity Natascha C. Perera, Karl-Heinz Wiesmüller, Maria Torp Larsen, Beate Schacher, Peter Eickholz, Niels Borregaard and Dieter E. Jenne DOI: http://dx.doi.org/10.1016/j.str.2014.07.008<ref> The residue F190 obstructs the active site which could normally not links a P1-Arg. However, a study[http://www.cell.com/structure/fulltext/S0969-2126(14)00238-X] considered the possibility that the two residues S216 and F190 of the active site can form a flexible gate which allows P1-Arg to enter. Then, the link between the active site and P1-Arg can be stabilized by a salt bridge interaction between S1-D226 and P1-Arg. The hypothesis of the flexible gate was confirmed by the same study. The mutations of S216 only, F190 only or both together show a forced full open gate is more efficient than a forced partially open gate. The conclusion is that the protease domain is a trypsin-like domain. </li></ol></ref>
