1hyl

<table><tr><td colspan='2'>[[1hyl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HYL FirstGlance]. <br>

</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=1hyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hyl OCA], [https://pdbe.org/1hyl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hyl RCSB], [https://www.ebi.ac.uk/pdbsum/1hyl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hyl ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/COGS_HYPLI COGS_HYPLI]] This enzyme is a serine protease capable of degrading the native triple helix of collagen. Also cleaves the B chain of insulin at the 15-Leu-|-Try-16 and 22-Arg-|-Gly-23 bonds. Hydrolyzes casein, but not Px-Pro-Leu-Gly-Pro-DArg, BzArgNHPh, AcTyrNHPh, 2-naphthyl phosphate, 2-naphthyl butyrate, 2-naphthyl caprylate, 2-naphthyl myristate, L-leucine 2-2-naphthylamide, L-valine 2-naphthylamide, L-cysteine 2-naphthylamide or L-glutarylphenylalanine 2-naphthylamide.<ref>PMID:230030</ref> <ref>PMID:2995028</ref>

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== Publication Abstract from PubMed ==

Collagenase from the fly larvae Hypoderma lineatum cleaves triple-helical collagen in a single region. It was crystallized at neutral pH in the absence of inhibitor and 1.8 A data were collected using synchrotron radiation and a Mark II prototype detector. The structure was solved by combining multiple isomorphous replacement methods and rotation translation function in real space. Refinement between 7 and 1.8 A using the program X-PLOR led to a final R factor of 16.9%. The overall fold is similar to that of other trypsin-like enzymes but the structure differs mainly by the presence of a beta-sheet at position 31-44. The two embedded molecules of the asymmetric unit are related by a pseudo twofold axis. The beta-sheet 31-44 of one molecule is involved in hydrogen bonds with binding-pocket residues of the other molecule. It thus completely prevents access to the active site. The specificity of this enzyme probably results from the position of Phe192 and Tyr99 at the entrance of the active site.

1.8 A structure of Hypoderma lineatum collagenase: a member of the serine proteinase family.,Broutin I, Arnoux B, Riche C, Lecroisey A, Keil B, Pascard C, Ducruix A Acta Crystallogr D Biol Crystallogr. 1996 Mar 1;52(Pt 2):380-92. PMID:15299709<ref>PMID:15299709</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1hyl" style="background-color:#fffaf0;"></div>

[[Category: Arnoux, B]]

[[Category: Broutin, I]]

[[Category: Ducruix, A]]

[[Category: Keil, B]]

[[Category: Lecroisey, A]]

[[Category: Pascard, C]]

[[Category: Riche, C]]