Ändra sökning
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Structure, specificity, and mode of interaction for bacterial albumin-binding modules
Visa övriga samt affilieringar
2002 (Engelska)Ingår i: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 277, nr 10, s. 8114-8120Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

We have determined the solution structure of an albumin binding domain of protein G, a surface protein of group C and G streptococci. We find that it folds into a left handed three-helix bundle similar to the albumin binding domain of protein PAB from Peptostreptococcus magnus. The two domains share 59% sequence identity, are thermally very stable, and bind to the same site on human serum albumin. The albumin binding site, the first determined for this structural motif known as the GA module, comprises residues spanning the first loop to the beginning of the third helix and includes the most conserved region of GA modules. The two GA modules have different affinities for albumin from different species, and their albumin binding patterns correspond directly to the host specificity of C/G streptococci and P. magnus, respectively. These studies of the evolution, structure, and binding properties of the GA module emphasize the power of bacterial adaptation and underline ecological and medical problems connected with the use of antibiotics.

Ort, förlag, år, upplaga, sidor
2002. Vol. 277, nr 10, s. 8114-8120
Nyckelord [en]
streptococcal protein-g, human-serum-albumin, igg-binding, immunoglobulin-g, b-domain, group-c, x-ray, nmr, evolution, identification
Identifikatorer
URN: urn:nbn:se:kth:diva-21366DOI: 10.1074/jbc.M109943200ISI: 000174268000063OAI: oai:DiVA.org:kth-21366DiVA, id: diva2:340064
Anmärkning
QC 20100525Tillgänglig från: 2010-08-10 Skapad: 2010-08-10 Senast uppdaterad: 2017-12-12Bibliografiskt granskad

Open Access i DiVA

Fulltext saknas i DiVA

Övriga länkar

Förlagets fulltext

Personposter BETA

Hober, SophiaUhlén, Mathias

Sök vidare i DiVA

Av författaren/redaktören
Hober, SophiaUhlén, Mathias
Av organisationen
Bioteknologi
I samma tidskrift
Journal of Biological Chemistry

Sök vidare utanför DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetricpoäng

doi
urn-nbn
Totalt: 31 träffar
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf