Structure and mode of action of microplusin, a copper II-chelating antimicrobial peptide from the cattle tick Rhipicephalus (Boophilus) microplus

Journal of Biological Chemistry

Volumn 284, Issue 50, 2009, Pages 34735-34746

  Silva, Fernanda D ^a   Rezende, Carlos A ^b   Rossi, Diego C P ^a   Esteves, Eliane ^a   Dyszy, Fábio H ^a   Schreier, Shirley ^a   Gueiros Filho, Frederico ^a   Campos, Cláudia B ^c   Pires, José R ^b   Daffre, Sirlei ^a,d  

^a UNIVERSITY OF SÃO PAULO   (Brazil)

^b FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

^c INSTITUTO DE PESQUISA E DESENVOLVIMENTO   (Brazil)

^d NONE   (Brazil)

Author keywords

[No Author keywords available]

Indexed keywords

ANTI-MICROBIAL ACTIVITY; ANTIBACTERIAL EFFECTS; ANTIMICROBIAL PEPTIDE; BACTERIAL MEMBRANES; BACTERIOSTATIC; CATTLE-TICKS; COPPER BINDING; CULTURE MEDIA; DEPENDENT PROCESS; FULLY REVERSED; GLOBULAR DOMAINS; GRAM-POSITIVE BACTERIUM; INNATE DEFENSE; MICROCOCCUS LUTEUS; MODE OF ACTION; NMR SPECTROSCOPY; PROTEIN BINDS; SOLUTION STRUCTURES;

AMINES; BACTERIA; BACTERIOLOGY; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES; SOLID SOLUTIONS;

COPPER;

CUPRIC ION; MICROPLUSIN; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIOSTASIS; BOOPHILUS MICROPLUS; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DRUG BINDING; DRUG DETERMINATION; DRUG STRUCTURE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; RESIDUE ANALYSIS; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; ANTIMICROBIAL CATIONIC PEPTIDES; BACTERIA; BINDING SITES; CATTLE; CIRCULAR DICHROISM; COPPER; HUMANS; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXYGEN CONSUMPTION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; RHIPICEPHALUS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS); BOOPHILUS; BOOPHILUS MICROPLUS; FUNGI; IXODIDA; MICROCOCCUS LUTEUS; POSIBACTERIA; RHIPICEPHALUS;

EID: 71749114416     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.016410     Document Type: Article

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