| Title |
On the Specificity of Heparin/Heparan Sulfate Binding to Proteins. Anion-Binding Sites on Antithrombin and Thrombin Are Fundamentally Different
|
|---|---|
| Published in |
PLOS ONE, November 2012
|
| DOI | 10.1371/journal.pone.0048632 |
| Pubmed ID | |
| Authors |
Philip D. Mosier, Chandravel Krishnasamy, Glen E. Kellogg, Umesh R. Desai |
| Abstract |
The antithrombin-heparin/heparan sulfate (H/HS) and thrombin-H/HS interactions are recognized as prototypic specific and non-specific glycosaminoglycan (GAG)-protein interactions, respectively. The fundamental structural basis for the origin of specificity, or lack thereof, in these interactions remains unclear. The availability of multiple co-crystal structures facilitates a structural analysis that challenges the long-held belief that the GAG binding sites in antithrombin and thrombin are essentially similar with high solvent exposure and shallow surface characteristics. |
Mendeley readers
The data shown below were compiled from readership statistics for 42 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Ukraine | 1 | 2% |
| Unknown | 41 | 98% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Researcher | 9 | 21% |
| Student > Master | 7 | 17% |
| Student > Ph. D. Student | 6 | 14% |
| Student > Bachelor | 5 | 12% |
| Professor | 4 | 10% |
| Other | 8 | 19% |
| Unknown | 3 | 7% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 10 | 24% |
| Chemistry | 7 | 17% |
| Agricultural and Biological Sciences | 7 | 17% |
| Medicine and Dentistry | 5 | 12% |
| Chemical Engineering | 2 | 5% |
| Other | 6 | 14% |
| Unknown | 5 | 12% |