2lu1 | pdb_00002lu1

pfsub2 solution NMR structure

spinqualitylabelsall models 2lu1 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lu1 is a 1 chain structure with sequence from Plasmodium falciparum. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SUB2_PLAFA Serine protease which plays an essential role in the shedding of AMA1, MSP1 and MSP7 from the surface of the invading merozoite; this step is essential for productive invasion and the release of the adhesion between the erythrocyte and the merozoite (PubMed:16322767). May cleave TRAMP/PTTRAMP, thereby shedding TRAMP from the merozoite surface during erythrocyte invasion (By similarity).[UniProtKB:Q8IHZ5] Publication Abstract from PubMed Plasmodium subtilisin 2 (Sub2) is a multi-domain protein that plays an important role in malaria infection. Here, we describe the solution NMR structure of a conserved region of the inhibitory prodomain of Sub2 from Plasmodium falciparum, termed prosub2. Despite the absence of any detectable sequence homology, the protozoan prosub2 has structural similarity to bacterial and mammalian subtilisin-like prodomains. Comparison with the three-dimensional structures of these other prodomains suggests a likely binding interface with the catalytic domain of Sub2 and provides insights into the locations of primary and secondary processing sites in Plasmodiumprodomains. Proteins 2012. (c) 2012 Wiley Periodicals, Inc. Solution NMR structure of a sheddase inhibitor prodomain from the malarial parasite Plasmodium falciparum.,He Y, Chen Y, Oganesyan N, Ruan B, O'Brochta D, Bryan PN, Orban J Proteins. 2012 Sep 26. doi: 10.1002/prot.24187. PMID:23011838 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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