Structural highlights
Function
[NP7_RHOPR] Converts nitrite as the sole substrate to form nitric oxide gas (NO). NO(2-) serves both as an electron donor and as an electron acceptor. Binds to negatively charged cell surfaces of activated platelets; binds to L-a-phosphatidyl-L-serine (PS)-bearing phospholipid membranes. Once bound on an activated platelet, NP7 releases its stored nitric oxide gas (NO) into the victim's tissues while feeding, resulting in vasodilation and inhibition of platelet aggregation. Also acts as an anticoagulant by blocking coagulation-factor binding sites. Has antihistamine activity; binds histamine with high affinity.[1] [2] [3] [4] [5]
References
- ↑ Andersen JF, Gudderra NP, Francischetti IM, Valenzuela JG, Ribeiro JM. Recognition of anionic phospholipid membranes by an antihemostatic protein from a blood-feeding insect. Biochemistry. 2004 Jun 8;43(22):6987-94. PMID:15170336 doi:https://dx.doi.org/10.1021/bi049655t
- ↑ Walker FA. Nitric oxide interaction with insect nitrophorins and thoughts on the electron configuration of the {FeNO}6 complex. J Inorg Biochem. 2005 Jan;99(1):216-36. PMID:15598503 doi:https://dx.doi.org/10.1016/j.jinorgbio.2004.10.009
- ↑ Knipp M, Zhang H, Berry RE, Walker FA. Overexpression in Escherichia coli and functional reconstitution of the liposome binding ferriheme protein nitrophorin 7 from the bloodsucking bug Rhodnius prolixus. Protein Expr Purif. 2007 Jul;54(1):183-91. Epub 2007 Mar 7. PMID:17428677 doi:https://dx.doi.org/10.1016/j.pep.2007.02.017
- ↑ Knipp M, Yang F, Berry RE, Zhang H, Shokhirev MN, Walker FA. Spectroscopic and functional characterization of nitrophorin 7 from the blood-feeding insect Rhodnius prolixus reveals an important role of its isoform-specific N-terminus for proper protein function. Biochemistry. 2007 Nov 20;46(46):13254-68. Epub 2007 Oct 24. PMID:17958381 doi:https://dx.doi.org/10.1021/bi7014986
- ↑ He C, Knipp M. Formation of nitric oxide from nitrite by the ferriheme b protein nitrophorin 7. J Am Chem Soc. 2009 Sep 2;131(34):12042-3. doi: 10.1021/ja9040362. PMID:19655755 doi:https://dx.doi.org/10.1021/ja9040362
