1rpc

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==Overview==
==Overview==
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The structure of RP 71955, a new tricyclic 21 amino acid peptide active, against human immunodeficiency virus 1, was determined. Its amino acid, composition was inferred from the results of fast atom bombardment mass, spectrometry, nuclear magnetic resonance, Raman spectroscopy, and amino, acid analysis. Its sequence could not be determined classically, using, Edman degradation, given the lack of a free terminal NH2. It was deduced, from the interpretation of interresidue nuclear Overhauser effects and, confirmed by the sequencing of peptides obtained by limited chemical, hydrolysis. It was found to be CLGIGSCNDFAGCGYAVVCFW. An internal amide, bond between the NH2 of C1 and the gamma-COOH of D9 was observed, as well, as two disulfide bridges, one between C1 and C13 and one between C7 and, C19. The three-dimensional structure of RP 71955 was determined from, nuclear magnetic resonance derived constraints using distance geometry, restrained molecular dynamics, nuclear Overhauser effect back calculation, and an iterative refinement using a full relaxation matrix approach., Analogies between the structure of RP 71955 and some functional domains of, gp41, the transmembrane protein of human immunodeficiency virus 1, suggest, hypotheses concerning the mode of action of RP 71955.
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The structure of RP 71955, a new tricyclic 21 amino acid peptide active against human immunodeficiency virus 1, was determined. Its amino acid composition was inferred from the results of fast atom bombardment mass spectrometry, nuclear magnetic resonance, Raman spectroscopy, and amino acid analysis. Its sequence could not be determined classically, using Edman degradation, given the lack of a free terminal NH2. It was deduced from the interpretation of interresidue nuclear Overhauser effects and confirmed by the sequencing of peptides obtained by limited chemical hydrolysis. It was found to be CLGIGSCNDFAGCGYAVVCFW. An internal amide bond between the NH2 of C1 and the gamma-COOH of D9 was observed, as well as two disulfide bridges, one between C1 and C13 and one between C7 and C19. The three-dimensional structure of RP 71955 was determined from nuclear magnetic resonance derived constraints using distance geometry, restrained molecular dynamics, nuclear Overhauser effect back calculation, and an iterative refinement using a full relaxation matrix approach. Analogies between the structure of RP 71955 and some functional domains of gp41, the transmembrane protein of human immunodeficiency virus 1, suggest hypotheses concerning the mode of action of RP 71955.
==About this Structure==
==About this Structure==
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[[Category: Faucher, D.]]
[[Category: Faucher, D.]]
[[Category: Frechet, D.]]
[[Category: Frechet, D.]]
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[[Category: Guitton, J.D.]]
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[[Category: Guitton, J D.]]
[[Category: Helynck, G.]]
[[Category: Helynck, G.]]
[[Category: Herman, F.]]
[[Category: Herman, F.]]
[[Category: James-Surcouf, E.]]
[[Category: James-Surcouf, E.]]
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[[Category: Ridoux, J.P.]]
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[[Category: Ridoux, J P.]]
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[[Category: Sorbier, B.Monegier.Du.]]
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[[Category: Sorbier, B Monegier Du.]]
[[Category: Vuilhorgne, M.]]
[[Category: Vuilhorgne, M.]]
[[Category: hiv replication inhibitor]]
[[Category: hiv replication inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:49:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:14 2008''

Revision as of 12:53, 21 February 2008


1rpc

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SOLUTION STRUCTURE OF RP 71955, A NEW 21 AMINO ACID TRICYCLIC PEPTIDE ACTIVE AGAINST HIV-1 VIRUS

Overview

The structure of RP 71955, a new tricyclic 21 amino acid peptide active against human immunodeficiency virus 1, was determined. Its amino acid composition was inferred from the results of fast atom bombardment mass spectrometry, nuclear magnetic resonance, Raman spectroscopy, and amino acid analysis. Its sequence could not be determined classically, using Edman degradation, given the lack of a free terminal NH2. It was deduced from the interpretation of interresidue nuclear Overhauser effects and confirmed by the sequencing of peptides obtained by limited chemical hydrolysis. It was found to be CLGIGSCNDFAGCGYAVVCFW. An internal amide bond between the NH2 of C1 and the gamma-COOH of D9 was observed, as well as two disulfide bridges, one between C1 and C13 and one between C7 and C19. The three-dimensional structure of RP 71955 was determined from nuclear magnetic resonance derived constraints using distance geometry, restrained molecular dynamics, nuclear Overhauser effect back calculation, and an iterative refinement using a full relaxation matrix approach. Analogies between the structure of RP 71955 and some functional domains of gp41, the transmembrane protein of human immunodeficiency virus 1, suggest hypotheses concerning the mode of action of RP 71955.

About this Structure

1RPC is a Single protein structure of sequence from Actinomycete sp9440. Full crystallographic information is available from OCA.

Reference

Solution structure of RP 71955, a new 21 amino acid tricyclic peptide active against HIV-1 virus., Frechet D, Guitton JD, Herman F, Faucher D, Helynck G, Monegier du Sorbier B, Ridoux JP, James-Surcouf E, Vuilhorgne M, Biochemistry. 1994 Jan 11;33(1):42-50. PMID:8286361

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