Journal:Acta Cryst F:S2053230X20000199
From Proteopedia
(Difference between revisions)
| Line 9: | Line 9: | ||
Overall Structure: The <scene name='83/833325/Cv/4'>overall structure of the protein</scene> adapts β-trefoil fold and this fold is known to be the signature of Kunitz type of protease inhibitors. A total of 179 residues of MP-4 form 12 β-strands arranged in β-hairpin like conformation connected by long loops. The tertiary structure is further stabilized by two disulphide bonds with the first one formed between residues <scene name='83/833325/Cv/6'>Cys45 and Cys90</scene> and the second one between <scene name='83/833325/Cv/7'>Cys145 and Cys152</scene>. | Overall Structure: The <scene name='83/833325/Cv/4'>overall structure of the protein</scene> adapts β-trefoil fold and this fold is known to be the signature of Kunitz type of protease inhibitors. A total of 179 residues of MP-4 form 12 β-strands arranged in β-hairpin like conformation connected by long loops. The tertiary structure is further stabilized by two disulphide bonds with the first one formed between residues <scene name='83/833325/Cv/6'>Cys45 and Cys90</scene> and the second one between <scene name='83/833325/Cv/7'>Cys145 and Cys152</scene>. | ||
| - | Functional Para: As the name suggests Kunitz type of protease inhibitors (KPTI) are responsible for inhibiting activity of certain proteases like trypsin. To inhibit proteases, the reactive site loop is known to occupy the active site groove of the target enzyme. The reactive site loop (RSL) is critical for its inhibitory activity and it extends from residue 66 to 74 and forms a loop in [[6jbp]]. The residue at the P1 position of the RSL is the principal residue that decides the inhibitory efficiency of protease inhibitor <ref name=Bode3>PMID:10708861</ref><ref name=Otlewski4>PMID:11732612</ref>. In functional KTPIs, the P1 position (69th residue) is usually occupied by Arg, Lys, Phe, Tyr, Leu or Met but the electron density map clearly shows that <scene name='83/833325/Cv/ | + | Functional Para: As the name suggests Kunitz type of protease inhibitors (KPTI) are responsible for inhibiting activity of certain proteases like trypsin. To inhibit proteases, the reactive site loop is known to occupy the active site groove of the target enzyme. <scene name='83/833325/Cv/8'>The reactive site loop (RSL) is critical for its inhibitory activity and it extends from residue 66 to 74</scene> and forms a loop in [[6jbp]]. The residue at the P1 position of the RSL is the principal residue that decides the inhibitory efficiency of protease inhibitor <ref name=Bode3>PMID:10708861</ref><ref name=Otlewski4>PMID:11732612</ref>. In functional KTPIs, the P1 position (69th residue) is usually occupied by Arg, Lys, Phe, Tyr, Leu or Met but the electron density map clearly shows that <scene name='83/833325/Cv/9'>the residue at this position is Ile</scene>. The presence of Ile at P1 position may be responsible for weak inhibitory activity exhibited by MP-4 <ref name=Salunke5>PMID:29330385</ref>. |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 09:20, 16 January 2020
| |||||||||||
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
