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1t7c

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Revision as of 08:03, 14 March 2018

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

Structural highlights

1t7c is a 4 chain structure with sequence from Bovin and Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1t8l, 1t8m, 1t8n, 1t8o, 1p2m, 1p2o, 1p2n, 1p2q, 1cbw, 1mtn
Activity:	Chymotrypsin, with EC number 3.4.21.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BPT1_BOVIN] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin.

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/1t7c"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF THE P1 GLU BPTI MUTANT- BOVINE CHYMOTRYPSIN COMPLEX==
 <StructureSection load='1t7c' size='340' side='right' caption='[[1t7c]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t8l|1t8l]], [[1t8m|1t8m]], [[1t8n|1t8n]], [[1t8o|1t8o]], [[1p2m|1p2m]], [[1p2o|1p2o]], [[1p2n|1p2n]], [[1p2q|1p2q]], [[1cbw|1cbw]], [[1mtn|1mtn]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7c OCA], [http://pdbe.org/1t7c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t7c RCSB], [http://www.ebi.ac.uk/pdbsum/1t7c PDBsum]</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=1t7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7c OCA], [http://pdbe.org/1t7c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t7c RCSB], [http://www.ebi.ac.uk/pdbsum/1t7c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t7c ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t7/1t7c_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t7/1t7c_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1t7c

From Proteopedia

Revision as of 08:03, 14 March 2018

CRYSTAL STRUCTURE OF THE P1 GLU 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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