Summary for 5KX4
| Entry DOI | 10.2210/pdb5kx4/pdb |
| Descriptor | 10.7 kDa salivary protein (2 entities in total) |
| Functional Keywords | insect protein, odorant-binding protein |
| Biological source | Lutzomyia longipalpis (Sand fly) |
| Total number of polymer chains | 2 |
| Total formula weight | 23848.30 |
| Authors | Asojo, O.A. (deposition date: 2016-07-20, release date: 2016-07-27, Last modification date: 2024-11-06) |
| Primary citation | Asojo, O.A.,Kelleher, A.,Liu, Z.,Pollet, J.,Hudspeth, E.M.,Rezende, W.C.,Groen, M.J.,Seid, C.A.,Abdeladhim, M.,Townsend, S.,de Castro, W.,Mendes-Sousa, A.,Bartholomeu, D.C.,Fujiwara, R.T.,Bottazzi, M.E.,Hotez, P.J.,Zhan, B.,Oliveira, F.,Kamhawi, S.,Valenzuela, J.G. Structure of SALO, a leishmaniasis vaccine candidate from the sand fly Lutzomyia longipalpis. PLoS Negl Trop Dis, 11:e0005374-e0005374, 2017 Cited by PubMed Abstract: Immunity to the sand fly salivary protein SALO (Salivary Anticomplement of Lutzomyia longipalpis) protected hamsters against Leishmania infantum and L. braziliensis infection and, more recently, a vaccine combination of a genetically modified Leishmania with SALO conferred strong protection against L. donovani infection. Because of the importance of SALO as a potential component of a leishmaniasis vaccine, a plan to produce this recombinant protein for future scale manufacturing as well as knowledge of its structural characteristics are needed to move SALO forward for the clinical path. PubMed: 28278244DOI: 10.1371/journal.pntd.0005374 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.94 Å) |
Structure validation
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