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Titolo:
Molecular modeling on human CCR5 receptors and complex with CD4 antigens and HIV-1 envelope glycoprotein gp120
Autore:
Yang, J; Liu, CQ;
Indirizzi:
Yunnan Univ, Modern Biol Ctr, Kunming 650091, Peoples R China Yunnan UnivKunming Peoples R China 650091 nming 650091, Peoples R China Chinese Acad Sci, Kunming Inst Zool, Lab Cellular & Mol Evolut, Kunming 650223, Peoples R China Chinese Acad Sci Kunming Peoples R China 650223 650223, Peoples R China
Titolo Testata:
ACTA PHARMACOLOGICA SINICA
fascicolo: 1, volume: 21, anno: 2000,
pagine: 29 - 34
SICI:
0253-9756(200001)21:1<29:MMOHCR>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
COFACTOR; ANTIBODY; CLONING; BINDING;
Keywords:
CCR5 receptors; CD4 antigens; HIV envelope protein; HIV-1; chemokine receptors; HLA antigens; molecular models;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
13
Recensione:
Indirizzi per estratti:
Indirizzo: Liu, CQ Yunnan Univ, Modern Biol Ctr, Kunming 650091, Peoples R China Yunnan Univ Kunming Peoples R China 650091 0091, Peoples R China
Citazione:
J. Yang e C.Q. Liu, "Molecular modeling on human CCR5 receptors and complex with CD4 antigens and HIV-1 envelope glycoprotein gp120", ACT PHAR SI, 21(1), 2000, pp. 29-34

Abstract

AIM: To investigate the interaction between human CCR5 receptors (CCR5) and HIV-1 envelope glycoprotein gp120 (HIV-1 gp120) and HIV-1 receptor CD4 antigens (CD4). METHODS: The structurally con served regions (SCR) of human CCR5 was built by the SYBYL/Biopolymer module using the corresponding transmembrane (TM) domain of bacteriorhodopsin (bR) as the template. The coordinates for amino-ter minal residue sequence, and carboxyl-terminal residue sequence, extracellular and cytoplasmic loops were generated using LOOP SEARCHalgorithm. Subsequently the structural model was merged into the complex with HIV-1 gp120 and CD4. RESULTS: Human CCR5 interacted with both an HIV-1 gp120 and CD4. The N-terminal residues (especially Met1 and Gln4) of human CCR5, contacted with CD4 residues, mainly 7Nith one span (56 - 59) of CD4 in electrostatic interaction and hydrogen-bonds. The binding sites of human CCR5 were buried in a hydrophobic center surrounded by a highly basic periphery. On the other hand, direct interatomic contacts were made between ? CCR5 residues and 6 gp120 amino-acid residues, which included van der Waals contacts, hydrophobic interaction, and hydrogen bonds. CONCLUSION: The interaction model should be helpful for rational design of novel anti-HIV drugs.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/04/20 alle ore 06:46:35