4hvp

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(New page: 200px<br /> <applet load="4hvp" size="450" color="white" frame="true" align="right" spinBox="true" caption="4hvp, resolution 2.3&Aring;" /> '''STRUCTURE OF COMPLEX...)
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<applet load="4hvp" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="4hvp, resolution 2.3&Aring;" />
caption="4hvp, resolution 2.3&Aring;" />
'''STRUCTURE OF COMPLEX OF SYNTHETIC HIV-1 PROTEASE WITH A STUBTRATE-BASED INHIBITOR AT 2.3 ANGSTROMS RESOLUTION'''<br />
'''STRUCTURE OF COMPLEX OF SYNTHETIC HIV-1 PROTEASE WITH A STUBTRATE-BASED INHIBITOR AT 2.3 ANGSTROMS RESOLUTION'''<br />
==Overview==
==Overview==
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The structure of a complex between a peptide inhibitor with the sequence, N-acetyl-Thr-Ile-Nle-psi[CH2-NH]-Nle-Gln-Arg.amide (Nle, norleucine) with, chemically synthesized HIV-1 (human immunodeficiency virus 1) protease was, determined at 2.3 A resolution (R factor of 0.176). Despite the symmetric, nature of the unliganded enzyme, the asymmetric inhibitor lies in a single, orientation and makes extensive interactions at the interface between the, two subunits of the homodimeric protein. Compared with the unliganded, enzyme, the protein molecule underwent substantial changes, particularly, in an extended region corresponding to the "flaps" (residues 35 to 57 in, each chain), where backbone movements as large as 7 A are observed.
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The structure of a complex between a peptide inhibitor with the sequence N-acetyl-Thr-Ile-Nle-psi[CH2-NH]-Nle-Gln-Arg.amide (Nle, norleucine) with chemically synthesized HIV-1 (human immunodeficiency virus 1) protease was determined at 2.3 A resolution (R factor of 0.176). Despite the symmetric nature of the unliganded enzyme, the asymmetric inhibitor lies in a single orientation and makes extensive interactions at the interface between the two subunits of the homodimeric protein. Compared with the unliganded enzyme, the protein molecule underwent substantial changes, particularly in an extended region corresponding to the "flaps" (residues 35 to 57 in each chain), where backbone movements as large as 7 A are observed.
==About this Structure==
==About this Structure==
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4HVP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with ACE and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4HVP OCA].
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4HVP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HVP OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Clawson, L.]]
[[Category: Clawson, L.]]
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[[Category: Kent, S.B.H.]]
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[[Category: Kent, S B.H.]]
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[[Category: Marshall, G.R.]]
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[[Category: Marshall, G R.]]
[[Category: Miller, M.]]
[[Category: Miller, M.]]
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[[Category: Sathyanarayana, B.K.]]
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[[Category: Sathyanarayana, B K.]]
[[Category: Schneider, J.]]
[[Category: Schneider, J.]]
[[Category: Selk, L.]]
[[Category: Selk, L.]]
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[[Category: Toth, M.V.]]
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[[Category: Toth, M V.]]
[[Category: Wlodawer, A.]]
[[Category: Wlodawer, A.]]
[[Category: ACE]]
[[Category: ACE]]
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[[Category: hydrolase(acid proteinase)]]
[[Category: hydrolase(acid proteinase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 14:58:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:34 2008''

Revision as of 17:13, 21 February 2008


4hvp, resolution 2.3Å

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STRUCTURE OF COMPLEX OF SYNTHETIC HIV-1 PROTEASE WITH A STUBTRATE-BASED INHIBITOR AT 2.3 ANGSTROMS RESOLUTION

Overview

The structure of a complex between a peptide inhibitor with the sequence N-acetyl-Thr-Ile-Nle-psi[CH2-NH]-Nle-Gln-Arg.amide (Nle, norleucine) with chemically synthesized HIV-1 (human immunodeficiency virus 1) protease was determined at 2.3 A resolution (R factor of 0.176). Despite the symmetric nature of the unliganded enzyme, the asymmetric inhibitor lies in a single orientation and makes extensive interactions at the interface between the two subunits of the homodimeric protein. Compared with the unliganded enzyme, the protein molecule underwent substantial changes, particularly in an extended region corresponding to the "flaps" (residues 35 to 57 in each chain), where backbone movements as large as 7 A are observed.

About this Structure

4HVP is a Single protein structure of sequence from Human immunodeficiency virus 1 with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of complex of synthetic HIV-1 protease with a substrate-based inhibitor at 2.3 A resolution., Miller M, Schneider J, Sathyanarayana BK, Toth MV, Marshall GR, Clawson L, Selk L, Kent SB, Wlodawer A, Science. 1989 Dec 1;246(4934):1149-52. PMID:2686029

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