1ylc
From Proteopedia
| Line 11: | Line 11: | ||
'''Trypsin/BPTI complex mutant''' | '''Trypsin/BPTI complex mutant''' | ||
| + | |||
| + | ==Overview== | ||
| + | Crystal structures, at 1.7 A resolution, were solved for complexes between each of two chemically synthesized partially folded analogues of bovine pancreatic trypsin inhibitor (BPTI) with the proteolytically inactive rat trypsin mutant S195A. The BPTI analogue termed [14-38](Abu) retains only the disulfide bond between Cys14 and Cys38, while Cys5, Cys30, Cys51, and Cys55 are replaced by isosteric alpha-amino-n-butyric acid residues. The analogue K26P,A27D[14-38](Abu) contains two further replacements, by statistically favored residues, in the type I beta-turn that has been suggested to be a main site for initiation of BPTI folding. As a control, the structure of the complex between S195A trypsin and wild-type BPTI was also solved. Despite significant differences in the degree of structure detected among these three BPTIs in solution by several biophysical techniques, their tertiary folds once bound to S195A trypsin in a crystalline lattice are essentially superimposable. | ||
==About this Structure== | ==About this Structure== | ||
1YLC is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YLC OCA]. | 1YLC is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YLC OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | Partially folded bovine pancreatic trypsin inhibitor analogues attain fully native structures when co-crystallized with S195A rat trypsin., Getun IV, Brown CK, Tulla-Puche J, Ohlendorf D, Woodward C, Barany G, J Mol Biol. 2008 Jan 18;375(3):812-23. Epub 2007 Nov 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18054043 18054043] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
| Line 20: | Line 26: | ||
[[Category: Ohlendorf, D H.]] | [[Category: Ohlendorf, D H.]] | ||
[[Category: Bpti]] | [[Category: Bpti]] | ||
| + | [[Category: Hydrolase/inhibitor complex]] | ||
[[Category: Pancreatic trypsin inhibitor]] | [[Category: Pancreatic trypsin inhibitor]] | ||
[[Category: Trypsin ii]] | [[Category: Trypsin ii]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 22:18:00 2008'' |
Revision as of 19:18, 22 May 2008
Trypsin/BPTI complex mutant
Overview
Crystal structures, at 1.7 A resolution, were solved for complexes between each of two chemically synthesized partially folded analogues of bovine pancreatic trypsin inhibitor (BPTI) with the proteolytically inactive rat trypsin mutant S195A. The BPTI analogue termed [14-38](Abu) retains only the disulfide bond between Cys14 and Cys38, while Cys5, Cys30, Cys51, and Cys55 are replaced by isosteric alpha-amino-n-butyric acid residues. The analogue K26P,A27D[14-38](Abu) contains two further replacements, by statistically favored residues, in the type I beta-turn that has been suggested to be a main site for initiation of BPTI folding. As a control, the structure of the complex between S195A trypsin and wild-type BPTI was also solved. Despite significant differences in the degree of structure detected among these three BPTIs in solution by several biophysical techniques, their tertiary folds once bound to S195A trypsin in a crystalline lattice are essentially superimposable.
About this Structure
1YLC is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Partially folded bovine pancreatic trypsin inhibitor analogues attain fully native structures when co-crystallized with S195A rat trypsin., Getun IV, Brown CK, Tulla-Puche J, Ohlendorf D, Woodward C, Barany G, J Mol Biol. 2008 Jan 18;375(3):812-23. Epub 2007 Nov 6. PMID:18054043 Page seeded by OCA on Thu May 22 22:18:00 2008
