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Atomic resolution structure of human HBP/CAP37/azurocidin
S Karlsen1, L F Iversen, I K Larsen
1Department of Medicinal Chemistry, Royal Danish School of Pharmacy, Universitetsparken 2, DK-2100 Copenhagen, Denmark. solveig.karlsen@chem.uit.no
Acta Crystallographica. Section D, Biological Crystallography
|October 8, 1998
Summary
This study presents the atomic-resolution crystal structure of human heparin-binding protein (HBP) at 1.1 Å. The findings reveal a potential protein kinase C activation site, offering new insights into HBP function.
Area of Science:
- Structural Biology
- Biochemistry
- Crystallography
Background:
- Human heparin-binding protein (HBP) is implicated in various biological processes.
- Previous structural studies of HBP were limited to lower resolution.
Purpose of the Study:
- To determine the high-resolution crystal structure of human HBP.
- To identify potential functional sites within the HBP structure.
Main Methods:
- X-ray crystallography of flash-frozen HBP crystals.
- Atomic resolution structure determination and anisotropic refinement using SHELXL96.
- Comparison with previously determined lower-resolution HBP structure.
Main Results:
- Obtained a 1.1 Å resolution structure of HBP.
- The final model includes 221 amino-acid residues, glycosylation units, ions, and solvent molecules.
- Identified a putative protein kinase C activation site (residues 113-120).
- Refined structure achieved R factor of 15.9% and Rfree of 18.9%.
Conclusions:
- The 1.1 Å resolution structure provides unprecedented detail of human HBP.
- The identified kinase activation site may be crucial for HBP's biological activity.
- This high-resolution structure serves as a valuable resource for further functional studies of HBP.