ATOMIC-RESOLUTION STRUCTURE OF HUMAN HBP CAP37/AZUROCIDIN/

Citation
S. Karlsen et al., ATOMIC-RESOLUTION STRUCTURE OF HUMAN HBP CAP37/AZUROCIDIN/, Acta crystallographica. Section D, Biological crystallography, 54, 1998, pp. 598-609
Citations number
33
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biophysics,Biology
ISSN journal
09074449
Volume
54
Year of publication
1998
Part
4
Pages
598 - 609
Database
ISI
SICI code
0907-4449(1998)54:<598:ASOHHC>2.0.ZU;2-9
Abstract
Crystals of human heparin binding protein (HBP) diffract to 1.1 Angstr om when flash-frozen at 120 K. The atomic resolution structure has bee n refined anisotropically using SHELXL96. The final model of HBP consi sts of 221 amino-acid residues of 225 possible, three glycosylation un its, one chloride ion, 15 precipitant ethanol molecules and 323 water molecules. The structure is refined to a final crystallographic R fact or of 15.9% and R-free(5%) of 18.9% using all data. A putative protein kinase C activation site has been identified, involving residues 113- 120. The structure is compared to the previously determined 2.3 Angstr om resolution structure of HBP.