6V4C

Culex quinquefasciatus D7 long form 1- CxD7L1 in complex with ADP

Summary for 6V4C

• Entry DOI: 10.2210/pdb6v4c/pdb
• Descriptor: Long form D7clu1 salivary protein, ADENOSINE-5'-DIPHOSPHATE, GLYCEROL, ... (8 entities in total)
• Functional Keywords: mosquito salivary protein, adp binding, d7 protein, protein binding
• Biological source: Culex quinquefasciatus (Southern house mosquito)
• Total number of polymer chains: 1
• Total formula weight: 34991.98

Authors

Calvo, E.,Garboczi, D.N.,Martin-Martin, I.,Gittis, A.G. (deposition date: 2019-11-27, release date: 2020-06-24, Last modification date: 2024-11-06)

Primary citation

Martin-Martin, I.,Paige, A.,Valenzuela Leon, P.C.,Gittis, A.G.,Kern, O.,Bonilla, B.,Chagas, A.C.,Ganesan, S.,Smith, L.B.,Garboczi, D.N.,Calvo, E.
ADP binding by the Culex quinquefasciatus mosquito D7 salivary protein enhances blood feeding on mammals.
Nat Commun, 11:2911-2911, 2020

PubMed Abstract: During blood-feeding, mosquito saliva is injected into the skin to facilitate blood meal acquisition. D7 proteins are among the most abundant components of the mosquito saliva. Here we report the ligand binding specificity and physiological relevance of two D7 long proteins from Culex quinquefasciatus mosquito, the vector of filaria parasites or West Nile viruses. CxD7L2 binds biogenic amines and eicosanoids. CxD7L1 exhibits high affinity for ADP and ATP, a binding capacity not reported in any D7. We solve the crystal structure of CxD7L1 in complex with ADP to 1.97 Å resolution. The binding pocket lies between the two protein domains, whereas all known D7s bind ligands either within the N- or the C-terminal domains. We demonstrate that these proteins inhibit hemostasis in ex vivo and in vivo experiments. Our results suggest that the ADP-binding function acquired by CxD7L1 evolved to enhance blood-feeding in mammals, where ADP plays a key role in platelet aggregation.

PubMed: 32518308
DOI: 10.1038/s41467-020-16665-z

Experimental method

X-RAY DIFFRACTION (1.97 Å)