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TitleDid evolution create a flexible ligand-binding cavity in the urokinase receptor through deletion of a plesiotypic disulfide bond?
Journal, issue, pagesJ Biol Chem, Vol. 294, Issue 18, Page 7403-7418, Year 2019
Publish dateMay 3, 2019
AuthorsJulie M Leth / Haydyn D T Mertens / Katrine Zinck Leth-Espensen / Thomas J D Jørgensen / Michael Ploug /
PubMed AbstractThe urokinase receptor (uPAR) is a founding member of a small protein family with multiple Ly6/uPAR (LU) domains. The motif defining these LU domains contains five plesiotypic disulfide bonds ...The urokinase receptor (uPAR) is a founding member of a small protein family with multiple Ly6/uPAR (LU) domains. The motif defining these LU domains contains five plesiotypic disulfide bonds stabilizing its prototypical three-fingered fold having three protruding loops. Notwithstanding the detailed knowledge on structure-function relationships in uPAR, one puzzling enigma remains unexplored. Why does the first LU domain in uPAR (DI) lack one of its consensus disulfide bonds, when the absence of this particular disulfide bond impairs the correct folding of other single LU domain-containing proteins? Here, using a variety of contemporary biophysical methods, we found that reintroducing the two missing half-cystines in uPAR DI caused the spontaneous formation of the corresponding consensus 7-8 LU domain disulfide bond. Importantly, constraints due to this cross-link impaired (i) the binding of uPAR to its primary ligand urokinase and (ii) the flexible interdomain assembly of the three LU domains in uPAR. We conclude that the evolutionary deletion of this particular disulfide bond in uPAR DI may have enabled the assembly of a high-affinity urokinase-binding cavity involving all three LU domains in uPAR. Of note, an analogous neofunctionalization occurred in snake venom α-neurotoxins upon loss of another pair of the plesiotypic LU domain half-cystines. In summary, elimination of the 7-8 consensus disulfide bond in the first LU domain of uPAR have significant functional and structural consequences.
External linksJ Biol Chem / PubMed:30894413 / PubMed Central
MethodsSAS (X-ray synchrotron)
Structure data

SASDF82:
Urokinase plasminogen activator surface receptor, uPAR H47C-N259C, complex with urokinase-type plasminogen activator (Amino Terminal Fragment, ATF).
Method: SAXS/SANS

SASDF92:
Urokinase plasminogen activator surface receptor, uPAR, T51C-V70C
Method: SAXS/SANS

SASDFA2:
Urokinase plasminogen activator surface receptor, uPAR T51C-V70C, complex with urokinase-type plasminogen activator (Amino Terminal Fragment, ATF).
Method: SAXS/SANS

SASDFB2:
Urokinase plasminogen activator surface receptor, uPAR, K50C-V70C
Method: SAXS/SANS

SASDFC2:
Urokinase plasminogen activator surface receptor, uPAR K50C-V70C, complex with urokinase-type plasminogen activator (Amino Terminal Fragment, ATF).
Method: SAXS/SANS

Source
  • Homo sapiens (human)

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