1t7c
From Proteopedia
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| - | [[Image:1t7c.gif|left|200px]] | + | [[Image:1t7c.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE P1 GLU BPTI MUTANT- BOVINE CHYMOTRYPSIN COMPLEX''' | + | {{Structure |
| + | |PDB= 1t7c |SIZE=350|CAPTION= <scene name='initialview01'>1t7c</scene>, resolution 1.85Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE P1 GLU BPTI MUTANT- BOVINE CHYMOTRYPSIN COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1T7C is a [ | + | 1T7C is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7C OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structures of five bovine chymotrypsin complexes with P1 BPTI variants., Czapinska H, Helland R, Smalas AO, Otlewski J, J Mol Biol. 2004 Dec 3;344(4):1005-20. PMID:[http:// | + | Crystal structures of five bovine chymotrypsin complexes with P1 BPTI variants., Czapinska H, Helland R, Smalas AO, Otlewski J, J Mol Biol. 2004 Dec 3;344(4):1005-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15544809 15544809] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Chymotrypsin]] | [[Category: Chymotrypsin]] | ||
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[[Category: chymotrypsin; serine proteinase; bovine pancreatic trypsin inhibitor; bpti; protein-protein interaction; non-cognate binding; s1 pocket; primary specificity; crystal structure]] | [[Category: chymotrypsin; serine proteinase; bovine pancreatic trypsin inhibitor; bpti; protein-protein interaction; non-cognate binding; s1 pocket; primary specificity; crystal structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:14:48 2008'' |
Revision as of 12:14, 20 March 2008
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| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Chymotrypsin, with EC number 3.4.21.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE P1 GLU BPTI MUTANT- BOVINE CHYMOTRYPSIN COMPLEX
Overview
The bovine chymotrypsin-bovine pancreatic trypsin inhibitor (BPTI) interaction belongs to extensively studied models of protein-protein recognition. The accommodation of the inhibitor P1 residue in the S1 binding site of the enzyme forms the hot spot of this interaction. Mutations introduced at the P1 position of BPTI result in a more than five orders of magnitude difference of the association constant values with the protease. To elucidate the structural aspects of the discrimination between different P1 residues, crystal structures of five bovine chymotrypsin-P1 BPTI variant complexes have been determined at pH 7.8 to a resolution below 2 A. The set includes polar (Thr), ionizable (Glu, His), medium-sized aliphatic (Met) and large aromatic (Trp) P1 residues and complements our earlier studies of the interaction of different P1 side-chains with the S1 pocket of chymotrypsin. The structures have been compared to the complexes of proteases with similar and dissimilar P1 preferences, including Streptomyces griseus proteases B and E, human neutrophil elastase, crab collagenase, bovine trypsin and human thrombin. The S1 sites of these enzymes share a common general shape of significant rigidity. Large and branched P1 residues adapt in their complexes similar conformations regardless of the polarity and size differences between their S1 pockets. Conversely, long and flexible residues such as P1 Met are present in the disordered form and display a conformational diversity despite similar inhibitory properties with respect to most enzymes studied. Thus, the S1 specificity profiles of the serine proteases appear to result from the precise complementarity of the P1-S1 interface and minor conformational adjustments occurring upon the inhibitor binding.
About this Structure
1T7C is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
Reference
Crystal structures of five bovine chymotrypsin complexes with P1 BPTI variants., Czapinska H, Helland R, Smalas AO, Otlewski J, J Mol Biol. 2004 Dec 3;344(4):1005-20. PMID:15544809
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