Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural and active site analysis of plasmepsins of Plasmodium falciparum: potential anti-malarial targets.

International journal of biological macromolecules - 30 Oct 2005

Bhargavi Rayavarapu, Sastry G Madhavi, Murty U Suryanarayana, Sastry G Narahari

Abstract excerpt

Comparative protein modeling, active site analysis and binding site specificity for the homologous series of plasmepsins (PM's), present in food vacuole of Plasmodium falciparum, are carried out. Four loops (L1, L2, L3 and L4), which show maximum structural deviations irrespective of type of inhibitor, have been identified. Comparison of the crystal structures of ligand complexes reveal that residues belonging to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antigens, Protozoan
Share to Antimalarials

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Aspartic Acid Endopeptidases

Share to Biophysics

Share to Catalytic Domain

Share to Lysine

Share to Models, Statistical

Share to Plasmodium falciparum

Source

Identifiers

PMID: 16242183
DOI: 10.1016/j.ijbiomac.2005.08.006

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and active site analysis of plasmepsins of Plasmodium falciparum: potential anti-malarial targets.PMID 16242183Read ↗

Computational Analysis of Luteolin, Apigenin and Their Derivatives from Allophylus africanus as Potential Inhibitors of Plasmepsin II a Malaria TargetSemantic proximity Read ↗

Structural rationale for the recognition of arginine at P₃ in PEXEL motif containing proteins of Plasmodium falciparum by plasmepsin V.Semantic proximity Read ↗

Bridging the Gap in Malaria Parasite Resistance, Current Interventions, and the Way Forward from in Silico Perspective: A ReviewSemantic proximity Read ↗

Hemoglobin Degrading Proteases of Plasmodium falciparum as Antimalarial Drug Targets.Semantic proximity Read ↗

Modeling and resistant alleles explain the selectivity of antimalarial compound 49c towards apicomplexan aspartyl proteases.Semantic proximity Read ↗

Imperfect duplicate insertions type of mutations in plasmepsin V modulates binding properties of PEXEL motifs of export proteins in Indian Plasmodium vivax.Semantic proximity Read ↗

<i>In silico</i> -based screening for natural product’s structural analogs as new drugs candidate against leishmaniasisSemantic proximity Read ↗

Computer-aided drug design approaches applied to screen natural product’s structural analogs targeting arginase in Leishmania sppSemantic proximity Read ↗

Structural modeling identifies Plasmodium vivax 4-diphosphocytidyl-2C-methyl-d-erythritol kinase (IspE) as a plausible new antimalarial drug target.Semantic proximity Read ↗

Homology Modeling and Docking Study of Shewanella Like Protein Phosphatase Involved in Development of Ookinetes in PlasmodiumSemantic proximity Read ↗

Crystal structure of calcium bound outer membrane phospholipase A (OmpLA) from <i>Salmonella typhi</i> and <i>in silico</i> anti-microbial screeningSemantic proximity Read ↗

Genomic landscape of the emerging XDR Salmonella Typhi for mining druggable targets clpP, hisH, folP and gpmI and screening of novel TCM inhibitors, molecular docking and simulation analysesSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.