1zfl

Solution structure of III-A, the major intermediate in the oxidative folding of leech carboxypeptidase inhibitor

spinqualitylabelsall models 1zfl, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1zfl is a 1 chain structure with sequence from Hirme. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1zfi, 1dtv, 1dtd Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MCPI_HIRME] Tightly binding, competitive inhibitor of different types of pancreatic-like carboxypeptidases. 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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