Webbläsaren som du använder stöds inte av denna webbplats. Alla versioner av Internet Explorer stöds inte längre, av oss eller Microsoft (läs mer här: * https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Var god och använd en modern webbläsare för att ta del av denna webbplats, som t.ex. nyaste versioner av Edge, Chrome, Firefox eller Safari osv.

Proposed lipocalin fold for apolipoprotein M based on bioinformatics and site-directed mutagenesis

Författare

Summary, in English

Apolipoprotein RI (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein, Sensitive sequence starches, threading and comparative model building experiments revealed apoM to be structurally related to the lipocalin protein family. In a 3D model, characterized by an eight-stranded anti-parallel beta -barrel, a segment including Asn135 could adopt a closed or open conformation. Using site-directed mutagenesis, we demonstrated Asn135 in wild-type apoM to be glycosylated, suggesting that the segment is solvent exposed, ApoM displays two strong acidic patches of potential functional importance, one around the N-terminus and the other next to the opening of the beta -barrel.

Publiceringsår

2001

Språk

Engelska

Sidor

127-132

Publikation/Tidskrift/Serie

FEBS Letters

Volym

499

Issue

1-2

Dokumenttyp

Artikel i tidskrift

Förlag

Wiley-Blackwell

Ämne

  • Biological Sciences

Nyckelord

  • Lipocalin
  • Apolipoprotein M
  • Comparative modeling
  • Site-directed mutagenesis

Status

Published

Forskningsgrupp

  • Clinical Chemistry, Malmö

ISBN/ISSN/Övrigt

  • ISSN: 1873-3468