1zfl
From Proteopedia
(Difference between revisions)
| (14 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1zfl.gif|left|200px]]<br /><applet load="1zfl" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1zfl" /> | ||
| - | '''Solution structure of III-A, the major intermediate in the oxidative folding of leech carboxypeptidase inhibitor'''<br /> | ||
| - | == | + | ==Solution structure of III-A, the major intermediate in the oxidative folding of leech carboxypeptidase inhibitor== |
| + | <StructureSection load='1zfl' size='340' side='right'caption='[[1zfl]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1zfl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZFL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZFL FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1zfl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zfl OCA], [https://pdbe.org/1zfl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zfl RCSB], [https://www.ebi.ac.uk/pdbsum/1zfl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zfl ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MCPI_HIRME MCPI_HIRME] Tightly binding, competitive inhibitor of different types of pancreatic-like carboxypeptidases. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The III-A intermediate constitutes the major rate-determining step in the oxidative folding of leech carboxypeptidase inhibitor (LCI). In this work, III-A has been directly purified from the folding reaction and structurally characterized by NMR spectroscopy. This species, containing three native disulfides, displays a highly native-like structure; however, it lacks some secondary structure elements, making it more flexible than native LCI. III-A represents a structurally determined example of a disulfide-insecure intermediate; direct oxidation of this species to the fully native protein seems to be restricted by the burial of its two free cysteine residues inside a native-like structure. We also show that theoretical approaches based on topological constraints predict with good accuracy the presence of this folding intermediate. Overall, the derived results suggest that, as it occurs with non-disulfide bonded proteins, native-like interactions between segments of secondary structure rather than the crosslinking of disulfide bonds direct the folding of LCI. | The III-A intermediate constitutes the major rate-determining step in the oxidative folding of leech carboxypeptidase inhibitor (LCI). In this work, III-A has been directly purified from the folding reaction and structurally characterized by NMR spectroscopy. This species, containing three native disulfides, displays a highly native-like structure; however, it lacks some secondary structure elements, making it more flexible than native LCI. III-A represents a structurally determined example of a disulfide-insecure intermediate; direct oxidation of this species to the fully native protein seems to be restricted by the burial of its two free cysteine residues inside a native-like structure. We also show that theoretical approaches based on topological constraints predict with good accuracy the presence of this folding intermediate. Overall, the derived results suggest that, as it occurs with non-disulfide bonded proteins, native-like interactions between segments of secondary structure rather than the crosslinking of disulfide bonds direct the folding of LCI. | ||
| - | + | NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor.,Arolas JL, D'Silva L, Popowicz GM, Aviles FX, Holak TA, Ventura S Structure. 2005 Aug;13(8):1193-202. PMID:16084391<ref>PMID:16084391</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1zfl" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Hirudo medicinalis]] | [[Category: Hirudo medicinalis]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Arolas | + | [[Category: Arolas JL]] |
| - | [[Category: Aviles | + | [[Category: Aviles FX]] |
| - | [[Category: | + | [[Category: D'Silva L]] |
| - | [[Category: | + | [[Category: Holak TA]] |
| - | [[Category: | + | [[Category: Popowicz GM]] |
| - | [[Category: Ventura | + | [[Category: Ventura S]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Solution structure of III-A, the major intermediate in the oxidative folding of leech carboxypeptidase inhibitor
| |||||||||||
