2LA1
Expression in Pichia pastoris and backbone dynamics of dendroaspin, a three finger toxin
Summary for 2LA1
| Entry DOI | 10.2210/pdb2la1/pdb |
| NMR Information | BMRB: 6915 |
| Descriptor | Mambin (1 entity in total) |
| Functional Keywords | dendroaspin, disintegrin, integrin, three-finger fold, snake toxin, toxin |
| Biological source | Dendroaspis jamesoni kaimosae (Eastern Jameson's mamba) |
| Cellular location | Secreted: P28375 |
| Total number of polymer chains | 1 |
| Total formula weight | 6761.68 |
| Authors | Chuang, W.J.,Cheng, C.H.,Chen, Y.C.,Shiu, J.H. (deposition date: 2011-03-01, release date: 2012-03-07, Last modification date: 2024-11-06) |
| Primary citation | Cheng, C.H.,Chen, Y.C.,Shiu, J.H.,Chang, Y.T.,Chang, Y.S.,Huang, C.H.,Chen, C.Y.,Chuang, W.J. Dynamics and functional differences between dendroaspin and rhodostomin: Insights into protein scaffolds in integrin recognition Protein Sci., 21:1872-1884, 2012 Cited by PubMed Abstract: Dendroaspin (Den) and rhodostomin (Rho) are snake venom proteins containing a PRGDMP motif. Although Den and Rho have different 3D structures, they are highly potent integrin inhibitors. To study their structure, function, and dynamics relationships, we expressed Den and Rho in Pichia pastoris. The recombinant Den and Rho inhibited platelet aggregation with the K(I) values of 149.8 and 83.2 nM. Cell adhesion analysis showed that Den was 3.7 times less active than Rho when inhibiting the integrin αIIbβ3 and 2.5 times less active when inhibiting the integrin αvβ3. In contrast, Den and Rho were similarly active when inhibiting the integrin α5β1 with the IC₅₀ values of 239.8 and 256.8 nM. NMR analysis showed that recombinant Den and Rho have different 3D conformations for their arginyl-glycyl-aspartic acid (RGD) motif. However, the comparison with Rho showed that the docking of Den into integrin αvβ3 resulted in a similar number of contacts. Analysis of the dynamic properties of the RGD loop in Den and Rho showed that they also had different dynamic properties. These results demonstrate that protein scaffolds affect the function, structure, and dynamics of their RGD motif. PubMed: 23033223DOI: 10.1002/pro.2169 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
