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1t8l

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CRYSTAL STRUCTURE OF THE P1 MET BPTI MUTANT- BOVINE CHYMOTRYPSIN COMPLEX

Structural highlights

1t8l is a 4 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.75Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CTRA_BOVIN

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

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Czapinska H, Helland R, Smalas AO, Otlewski J. Crystal structures of five bovine chymotrypsin complexes with P1 BPTI variants. J Mol Biol. 2004 Dec 3;344(4):1005-20. PMID:15544809 doi:10.1016/j.jmb.2004.09.088

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1t8l"

@@ Line 3: / Line 3: @@
 <StructureSection load='1t8l' size='340' side='right'caption='[[1t8l]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1t8l]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T8L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T8L FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1t8l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T8L FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t7c|1t7c]], [[1t8m|1t8m]], [[1t8n|1t8n]], [[1t8o|1t8o]], [[1p2m|1p2m]], [[1p2o|1p2o]], [[1p2n|1p2n]], [[1p2q|1p2q]], [[1cbw|1cbw]], [[1mtn|1mtn]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t8l OCA], [https://pdbe.org/1t8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t8l RCSB], [https://www.ebi.ac.uk/pdbsum/1t8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t8l ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t8l OCA], [http://pdbe.org/1t8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t8l RCSB], [http://www.ebi.ac.uk/pdbsum/1t8l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t8l ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/BPT1_BOVIN BPT1_BOVIN]] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin.
+[https://www.uniprot.org/uniprot/CTRA_BOVIN CTRA_BOVIN]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 39: / Line 38: @@
 </StructureSection>
 [[Category: Bos taurus]]
-[[Category: Bovin]]
-[[Category: Chymotrypsin]]
 [[Category: Large Structures]]
-[[Category: Czapinska, H]]
+[[Category: Czapinska H]]
-[[Category: Helland, R]]
+[[Category: Helland R]]
-[[Category: Otlewski, J]]
+[[Category: Otlewski J]]
-[[Category: Smalas, A O]]
+[[Category: Smalas AO]]
-[[Category: Bovine pancreatic trypsin inhibitor]]
-[[Category: Bpti]]
-[[Category: Crystal structure]]
-[[Category: Hydrolase-hydrolase inhibitor complex]]
-[[Category: Non-cognate binding]]
-[[Category: Primary specificity]]
-[[Category: Protein-protein interaction]]
-[[Category: S1 pocket]]
-[[Category: Serine proteinase]]

1t8l

From Proteopedia

Current revision

CRYSTAL STRUCTURE OF THE P1 MET BPTI MUTANT- BOVINE CHYMOTRYPSIN COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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