1uhb
From Proteopedia
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Crystal structure of porcine alpha trypsin bound with auto catalyticaly produced native peptide at 2.15 A resolution
Overview
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.
About this Structure
1UHB is a Protein complex structure of sequences from Sus scrofa with ACT and CA as ligands. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 04:07:34 2007
