1lpc is a 1 chain structure with sequence from Dianthus caryophyllus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Dianthin antiviral protein (DAP) is a naturally occurring antiviral protein from the leaves of carnation (Dianthus caryophyllus) capable of depurinating HIV-1 RNA and inhibiting HIV-1 replication in human peripheral blood mononuclear cells. Escherichia coli-derived recombinant DAP (rDAP, amino acids 1-254) was purified to homogeneity for structural and functional studies. In the following paper the X-ray crystal structure of rDAP as well as its complexes with cyclic AMP and adenyl-guanosine (ApG) as substrate analogs at 1.7 A resolution are reported. Molecular modeling studies of the interactions of DAP and the structurally similar pokeweed antiviral protein (PAP) with a single-stranded RNA heptamer predicted a more potent anti-HIV activity for rDAP due to its unique surface topology and more favorable charge distribution in its 20 A-long RNA binding active center cleft. In accordance with the predictions of the modeling studies, rDAP was more potent than rPAP in depurinating HIV-1 RNA. To the knowledge of the authors, this is the first structural and functional characterization of recombinant DAP.
High resolution X-ray structure and potent anti-HIV activity of recombinant dianthin antiviral protein.,Kurinov IV, Rajamohan F, Uckun FM Arzneimittelforschung. 2004;54(10):692-702. PMID:15553110[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Kurinov IV, Rajamohan F, Uckun FM. High resolution X-ray structure and potent anti-HIV activity of recombinant dianthin antiviral protein. Arzneimittelforschung. 2004;54(10):692-702. PMID:15553110
