- AutorIn
- Jan Pippel
- E. Bartholomeus Kuettner
- David Ulbricht
- Jan Daberger
- Stephan Schultz
- John T. Heiker
- Norbert Sträter
- Titel
- Crystal structure of cleaved vaspin (serpinA12)
- Zitierfähige Url:
- https://nbn-resolving.org/urn:nbn:de:bsz:15-qucosa2-334386
- Quellenangabe
- Biological Chemistry
Erscheinungsjahr: 2016
Jahrgang: 397
Heft: 2
Seiten: 111-123
ISSN: 1437-4315 - Erstveröffentlichung
- 2016
- Abstract (EN)
- The adipokine vaspin (serpinA12) is mainly expressed in white adipose tissue and exhibits various beneficial effects on obesity-related processes. Kallikrein 7 is the only known target protease of vaspin and is inhibited by the classical serpin inhibitory mechanism involving a cleavage of the reactive center loop between P1 (M378) and P1′ (E379). Here, we present the X-ray structure of vaspin, cleaved between M378 and E379. We provide a comprehensive analysis of differences between the uncleaved and cleaved forms in the shutter, breach, and hinge regions with relation to common molecular features underlying the serpin inhibitory mode. Furthermore, we point out differences towards other serpins and provide novel data underlining the remarkable stability of vaspin. We speculate that the previously reported FKGx1Wx2x3 motif in the breach region may play a decisive role in determining the reactive center loop configuration in the native vaspin state and might contribute to the high thermostability of vaspin. Thus, this structure may provide a basis for future mutational studies.
- Andere Ausgabe
- Link zur Originalpublikation
DOI: 10.1515/hsz-2015-0229
Link: https://www.degruyter.com/view/j/bchm.2016.397.issue-2/hsz-2015-0229/hsz-2015-0229.xml - Freie Schlagwörter (EN)
- Cleaved serpin; Kallikrein 7; Reactive center loop; Vaspin; X-ray structure
- Klassifikation (DDC)
- 572
- Verlag
- De Gruyter, Berlin
- Version / Begutachtungsstatus
- angenommene Version / Postprint / Autorenversion
- URN Qucosa
- urn:nbn:de:bsz:15-qucosa2-334386
- Veröffentlichungsdatum Qucosa
- 06.03.2019
- Dokumenttyp
- Artikel
- Sprache des Dokumentes
- Englisch
- Lizenz / Rechtehinweis