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Literature summary for 3.4.22.B49 extracted from

  • Nandy, S.K.; Seal, A.
    Structural dynamics investigation of human family 1 & 2 cystatin-cathepsin L1 interaction a comparison of binding modes (2016), PLoS ONE, 11, e0164970 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.B49

Inhibitors

Inhibitors Comment Organism Structure
cystatin C
-
 Homo sapiens
cystatin D
-
 Homo sapiens
cystatin F
-
 Homo sapiens
cystatin M/E
-
 Homo sapiens
Cystatin S
-
 Homo sapiens
cystatin SA
-
 Homo sapiens
cystatin SN
-
 Homo sapiens
additional information inhibitory interactions of human family 1 and 2 cystatins with cathepsin L1 are predicted and their stability and viability are verified through protein docking and comparative molecular dynamics, overview. The key amino acid residues surfaced via interaction energy, hydrogen bonding and solvent accessible surface area analysis for each cystatin-cathepsin L1 complex influence the mode of binding and thus control the diverse inhibitory affinity of cystatins towards cysteine proteases. Docking outputs of cathepsin L1 complexes with stefin A, stefin B, cystatin C, cystatin D, cystatin F, cystatin M/E, cystatin S, cystatin SA, and cystatin SN Homo sapiens
Stefin A
-
 Homo sapiens
Stefin B
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P07711
-
-

Synonyms

Synonyms Comment Organism
CL1
-
 Homo sapiens