Atomic resolution structure of human HBP/CAP37/azurocidin.
Crystals of human heparin binding protein (HBP) diffract to 1.1 A when flash-frozen at 120 K. The atomic resolution structure has been refined anisotropically using SHELXL96. The final model of HBP consists of 221 amino-acid residues of 225 possible, three glycosylation units, one chloride ion, 15 precipitant ethanol molecules and 323 water molecules. The structure is refined to a final crystallographic R factor of 15.9% and Rfree(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 A resolution structure of HBP.
Karlsen
S
S
Department of Medicinal Chemistry, Royal Danish School of Pharmacy, Universitetsparken 2, DK-2100 Copenhagen, Denmark. solveig.karlsen@chem.uit.no
Iversen
L F
LF
Larsen
I K
IK
Flodgaard
H J
HJ
Kastrup
J S
JS
D023181:Antimicrobial Cationic Peptides; D001665:Binding Sites; D001798:Blood Proteins / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004789:Enzyme Activation; D006031:Glycosylation; D006358:Hot Temperature; D006801:Humans; D008050:Lipid A / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D011493:Protein Kinase C / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D013329:Structure-Activity Relationship
C062991:AZU1 protein, human; D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins; D002352:Carrier Proteins; D008050:Lipid A; D011493:Protein Kinase C