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==Structure of mutant human cathepsin L, engineered for GAG binding==
==Structure of mutant human cathepsin L, engineered for GAG binding==
<StructureSection load='6jd0' size='340' side='right'caption='[[6jd0]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
<StructureSection load='6jd0' size='340' side='right'caption='[[6jd0]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6jd0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JD0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6jd0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JD0 FirstGlance]. <br>
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/CATL1_HUMAN CATL1_HUMAN] Important for the overall degradation of proteins in lysosomes.
[https://www.uniprot.org/uniprot/CATL1_HUMAN CATL1_HUMAN] Important for the overall degradation of proteins in lysosomes.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Engineering precise substrate specificity of proteases advances the potential to use them in biotechnological and therapeutic applications. Collagen degradation, a physiological process mediated by collagenases, is an integral part of extracellular matrix remodeling and when uncontrolled, implicated in different pathological conditions. Lysosomal cathepsin-K cleaves triple helical collagen fiber, whereas cathepsin-L cannot do so. In this study, we have imparted collagenolytic property to cathepsin-L, by systematically engineering proline-specificity and glycosaminoglycans (GAG)-binding surface in the protease. The proline-specific mutant shows high specificity for prolyl-peptidic substrate but is incapable of cleaving collagen. Engineering a GAG-binding surface on the proline-specific mutant enabled it to degrade type-I collagen in the presence of chondroitin-4-sulfate (C4-S). We also present the crystal structures of proline-specific (1.4 A) and collagen-specific (1.8 A) mutants. Finally docking studies with prolyl-peptidic substrate (Ala-Gly-Pro-Arg-Ala) at the active site and a C4-S molecule at the GAG-binding site enable us to identify key structural features responsible for collagenolytic activity of cysteine cathepsins.
Structure-guided protein engineering of human cathepsin L for efficient collagenolytic activity.,Choudhury D, Biswas S Protein Eng Des Sel. 2021 Feb 15;34. pii: 6213762. doi: 10.1093/protein/gzab005. PMID:33825882<ref>PMID:33825882</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jd0" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cathepsin 3D structures|Cathepsin 3D structures]]
*[[Cathepsin 3D structures|Cathepsin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 11:09, 30 October 2024

Structure of mutant human cathepsin L, engineered for GAG binding

6jd0, resolution 1.80Å

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