1bxf: Difference between revisions
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<StructureSection load='1bxf' size='340' side='right'caption='[[1bxf]]' scene=''> | <StructureSection load='1bxf' size='340' side='right'caption='[[1bxf]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BXF FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=1bxf FirstGlance], [https://www.ebi.ac.uk/pdbsum/1bxf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bxf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Latest revision as of 13:30, 14 July 2021
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THREE-DIMENSIONAL STRUCTURES OF THE CYSTEINE-PROTEASES CATHEPSINS K AND S DEDUCED BY KNOWLEDGE-BASED MODELLING AND ACTIVE-SITE CHARACTERISTICSTHREE-DIMENSIONAL STRUCTURES OF THE CYSTEINE-PROTEASES CATHEPSINS K AND S DEDUCED BY KNOWLEDGE-BASED MODELLING AND ACTIVE-SITE CHARACTERISTICS
Structural highlights
Publication Abstract from PubMedHuman cathepsins K and S are recently identified proteins with high primary sequence homology to members of papain superfamily, including cathepsins B, L, H and papain. Models of the tertiary structures of cathepsins K and S and their complexes with a specific substrate and inhibitor were constructed and compared with the recently determined X-ray structure of cathepsin K. A major problem in the determination of the three-dimensional structure of proteins concerns the quality of the structural models obtained from the interpretation of experimental data. The framework of the tertiary structures of cathepsins K and S consisted of structurally conserved regions from the tertiary structure of the papain superfamily and the variable regions were constructed with fragments of other proteins from the protein data base. Based on docking studies the non-bonded interaction energies of ligands with the cathepsins were estimated. These energies correlate with experimentally determined substrate and inhibitory potency. Three-dimensional structures of the cysteine proteases cathepsins K and S deduced by knowledge-based modelling and active site characteristics.,Fengler A, Brandt W Protein Eng. 1998 Nov;11(11):1007-13. PMID:9876921[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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