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Information Seminar Paper

Title

LOMEFLOXACIN PROMOTES THE INTERACTION BETWEEN HOLO TRANSFERRIN IN THE DETERMINATION OF THE BINDING MECHANISM BY MOLECULAR MODELING TECHNIQUE

Pages

 Start Page | End Page

Keywords

DENSITY FUNCTIONAL THEORY (DFT) 

Abstract

 HUMAN HOLO TRANSFRRIN (HTF) IS ONE OF THE MONOMERIC SERUM PROTEINS OF FAMILY TF THAT CONSIST OF A SINGLE_CHAIN GLYCOPROTEIN WITH 679 AMINO ACID RESIDU THAT PROTEIN CONTAINING TWO CHAINS, EACH CHAIN HAS THREE TRP RESIDUES. THE CRYSTAL STRUCTURE OF HUMAN TRANSFERRIN IN COMPLEX WITH ITS RECEPTOR WAS RETRIEVED FROM PDB. OUT OF THE ENTRIES (1BTJ) FOR HTF FROM RCSB PROTEIN DATA BANK (HTTP: //WWW.RCSB. ORG/PDB).A THOROUGH UNDERSTANDING OF THE STRUCTURAL PRINCIPLES THAT ESTIMATING THE STRENGTH OF A PROTEIN-LIGAND COMPLEX, AN ACCURATE AND FAST DOCKING PROTOCOL AND THE ABILITY TO VISUALIZE BINDING GEOMETRIES AND INTERACTIONS ARE MANDATORY. THUS WE STUDY THE INTERACTIONS OF HTF AND LAMEFLOXACIN BY MEANS OF AUTODOCK AND DENSITY FUNCTIONAL THEORY (DFT). THE DOCKED POSE OF THESE MOLECULES SHOWED THAT FOLLOWING TRENDS AFFINITY TO LMF: TRP264 (B)>TRP128 (A) TYR71 (B)>TYR45 (A)>TYR223 (A)>TYR 314 (A)>TYR 136 (A)>TYR 185 (B)>TYR 238 (B).

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