Structural highlights
Function
Q63T97_BURPS
Publication Abstract from PubMed
We report the structural and functional characterization of a novel heparanase (BpHep) from the invasive pathogenic bacterium Burkholderia pseudomallei (Bp), showing approximately 24% sequence identity with human heparanase (hHep). Site-directed mutagenesis studies confirmed the active site resi-dues essential for activity, and we found that BpHep has specificity for heparan sulfate. Finally, we describe the first heparanase X-ray crystal structure, which provides new insight into both substrate recognition and inhibitor design.
Functional and structural characterization of a heparanase.,Bohlmann L, Tredwell GD, Yu X, Chang CW, Haselhorst T, Winger M, Dyason JC, Thomson RJ, Tiralongo J, Beacham IR, Blanchard H, von Itzstein M Nat Chem Biol. 2015 Dec;11(12):955-7. doi: 10.1038/nchembio.1956. Epub 2015 Nov, 2. PMID:26565989[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bohlmann L, Tredwell GD, Yu X, Chang CW, Haselhorst T, Winger M, Dyason JC, Thomson RJ, Tiralongo J, Beacham IR, Blanchard H, von Itzstein M. Functional and structural characterization of a heparanase. Nat Chem Biol. 2015 Dec;11(12):955-7. doi: 10.1038/nchembio.1956. Epub 2015 Nov, 2. PMID:26565989 doi:http://dx.doi.org/10.1038/nchembio.1956
