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1a30

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[[Image:1a30.gif|left|200px]]
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{{STRUCTURE_1a30| PDB=1a30 | SCENE= }}
{{STRUCTURE_1a30| PDB=1a30 | SCENE= }}
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'''HIV-1 PROTEASE COMPLEXED WITH A TRIPEPTIDE INHIBITOR'''
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===HIV-1 PROTEASE COMPLEXED WITH A TRIPEPTIDE INHIBITOR===
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==Overview==
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The HIV-1 transframe region (TFR) is between the structural and functional domains of the Gag-Pol polyprotein, flanked by the nucleocapsid and the protease domains at its N and C termini, respectively. Transframe octapeptide (TFP) Phe-Leu-Arg-Glu-Asp-Leu-Ala-Phe, the N terminus of TFR, and its analogues are competitive inhibitors of the action of the mature HIV-1 protease. The smallest, most potent analogues are tripeptides: Glu-Asp-Leu and Glu-Asp-Phe with Ki values of approximately 50 and approximately 20 microM, respectively. Substitution of the acidic amino acids in the TFP by neutral amino acids and d or retro-d configurations of Glu-Asp-Leu results in an &gt;40-fold increase in Ki. Protease inhibition by Glu-Asp-Leu is dependent on a protonated form of a group with a pKa of 3.8; unlike other inhibitors of HIV-1 protease which are highly hydrophobic, Glu-Asp-Leu is extremely soluble in water, and its binding affinity decreases with increasing NaCl concentration. However, Glu-Asp-Leu is a poor inhibitor (Ki approximately 7.5 mM) of the mammalian aspartic acid protease pepsin. X-ray crystallographic studies at pH 4.2 show that the interactions of Glu at P2 and Leu at P1 of Glu-Asp-Leu with residues of the active site of HIV-1 protease are similar to those of other product-enzyme complexes. It was not feasible to understand the interaction of intact TFP with HIV-1 protease under conditions of crystal growth due to its hydrolysis giving rise to two products. The sequence-specific, selective inhibition of the HIV-1 protease by the viral TFP suggests a role for TFP in regulating protease function during HIV-1 replication.
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(as it appears on PubMed at http://www.pubmed.gov), where 9485357 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9485357}}
==About this Structure==
==About this Structure==
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[[Category: Aspartic protease]]
[[Category: Aspartic protease]]
[[Category: Hiv protease]]
[[Category: Hiv protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:53:19 2008''

Revision as of 12:53, 30 June 2008

Image:1a30.png

Template:STRUCTURE 1a30

HIV-1 PROTEASE COMPLEXED WITH A TRIPEPTIDE INHIBITOR

Template:ABSTRACT PUBMED 9485357

About this Structure

1A30 is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

Reference

Hydrophilic peptides derived from the transframe region of Gag-Pol inhibit the HIV-1 protease., Louis JM, Dyda F, Nashed NT, Kimmel AR, Davies DR, Biochemistry. 1998 Feb 24;37(8):2105-10. PMID:9485357

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