Structural highlights
Function
TRYP_PIG
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Trypsin, a serine protease enzyme plays a pivotal role in digestion and is autocatalytic. The crystal structure of a complex formed between porcine trypsin and an auto catalytically produced peptide is reported here. This complex shows a reduction in enzyme activity as compared to native beta-trypsin. The nonapeptide has a lysine, which is recognized by Asp 189 at the specificity pocket. The auto catalytically produced native nonapeptide is bound at the active site cleft like other trypsin inhibitors but the important interactions with the oxyanion hole are absent. The peptide covers only a part of the active site cleft and hence the enzyme activity is reduced rather than being inhibited.
Trypsin activity reduced by an autocatalytically produced nonapeptide.,Ibrahim BS, Shamaladevi N, Pattabhi V J Biomol Struct Dyn. 2004 Jun;21(6):737-44. PMID:15106996[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ibrahim BS, Shamaladevi N, Pattabhi V. Trypsin activity reduced by an autocatalytically produced nonapeptide. J Biomol Struct Dyn. 2004 Jun;21(6):737-44. PMID:15106996
