2013
DOI: 10.1080/07391102.2012.706403
|View full text |Cite
|
Sign up to set email alerts
|

Modelling family 2 cystatins and their interaction with papain

Abstract: Cystatins are extensively studied cysteine protease inhibitors, found in wide range of organisms with highly conserved structural folds. S-type of cystatins is well known for their abundance in saliva, high selectivity and poorer activity towards host cysteine proteases in comparison to their immediate ancestor cystatin C. Despite more than 90% sequence similarity, the members of this group show highly dissimilar binding affinity towards papain. Cystatin M/E is a potent inhibitor of legumain and papain like cy… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
12
0

Year Published

2015
2015
2024
2024

Publication Types

Select...
8
1

Relationship

0
9

Authors

Journals

citations
Cited by 17 publications
(13 citation statements)
references
References 87 publications
1
12
0
Order By: Relevance
“…Likewise, the docking of TcCYSPR04 and TcCYS4 has showed electrostatic complementarities of the surface contact ( Fig 8 ). The same was observed for papain and cystatin S from saliva [ 9 ].…”
Section: Discussionsupporting
confidence: 73%
See 1 more Smart Citation
“…Likewise, the docking of TcCYSPR04 and TcCYS4 has showed electrostatic complementarities of the surface contact ( Fig 8 ). The same was observed for papain and cystatin S from saliva [ 9 ].…”
Section: Discussionsupporting
confidence: 73%
“…Therefore, the interaction of proteases with their substrates and inhibitors can be seen as a molecular battlefield [ 7 ]. The structure of the complex between exogenous papain and cystatin is well analyzed [ 8 , 9 ], but little is known about the interaction between PLCP and cystatin in the same organism.…”
Section: Introductionmentioning
confidence: 99%
“…A 500 ps NVT equilibration was performed at temperature of 300 K with position restraints applied to protein and ligand in order to relieve any bad contacts at the residues solvent interface [50]. Then a 1000 ps NPT simulation was conducted, and pressure was coupled to 1.0 atm using the Parrinello−Rahman method.…”
Section: Methodsmentioning
confidence: 99%
“…On the other hand, the acidic pH may also affect the structure of papain. In this sense, the area of contact between the cystatin and the target proteases, in the models of docking, involves hydrophobic and ionic interactions that may be affected by variations in pH [ 36 ]. In addition, many proteins do not support great variations in pH, with denaturation occurring at extreme pH ranges; however, T cCYS4 supported a wide range of variation of pH without losing its inhibitory power completely, proving to be more sensitive to extremely acidic pHs.…”
Section: Discussionmentioning
confidence: 99%