2JOO
The NMR Solution Structure of Recombinant RGD-hirudin
Summary for 2JOO
| Entry DOI | 10.2210/pdb2joo/pdb |
| NMR Information | BMRB: 15405 |
| Descriptor | Hirudin variant-1 (1 entity in total) |
| Functional Keywords | mainly beta, blood clotting |
| Biological source | Hirudo medicinalis (medicinal leech) |
| Cellular location | Secreted: P01050 |
| Total number of polymer chains | 1 |
| Total formula weight | 7042.59 |
| Authors | |
| Primary citation | Song, X.,Mo, W.,Liu, X.,Zhu, L.,Yan, X.,Song, H.,Dai, L. The NMR solution structure of recombinant RGD-hirudin Biochem.Biophys.Res.Commun., 360:103-108, 2007 Cited by PubMed Abstract: The solution structure of a new recombinant RGD-hirudin, which has the activities of anti-thrombin and anti-platelet aggregation, was determined by (1)H nuclear magnetic resonance spectroscopy and compared with the conformations of recombinant wild-type hirudin and hirudin (variant 2, Lys47) of the hirudin thrombin complex. On the basis of total 1284 distance and dihedral angle constraints derived from a series of NMR spectra, 20 conformers were computed with ARIA/CNS programs. The structure of residues 3-30 and 37-48 form a molecular core with two antiparallel beta-sheets as the other two hirudins. However, significant differences were found in the surface electrostatic charge distributions among the three hirudins, especially in the RGD segment of recombinant RGD-hirudin. This difference may be greatly beneficial to its additional function of anti-platelet aggregation. The difference in extended C-terminal makes its both ionic and hydrophobic interactions with the fibrinogen recognition exosite of thrombin more effective. PubMed: 17585879DOI: 10.1016/j.bbrc.2007.06.014 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
