cd05482

Retropepsins, pepsin-like aspartate proteases

CDD entry
Member databaseCDD
CDD typedomain
Short nameHIV_retropepsin_like
Setpepsin_retropepsin_like

Description

This is a subfamily of retropepsins. The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A.
[2, 7, 3, 6, 4, 5, 1]

References

1.[Retroviruses-derived sequences in the human genome. Human endogenous retroviruses (HERVs)]. Zwolinska K. Postepy Hig Med Dosw (Online) 60, 637-52, (2006). PMID: 17199106

2.Three-dimensional structures of HIV-1 and SIV protease product complexes. Rose RB, Craik CS, Douglas NL, Stroud RM. Biochemistry 35, 12933-44, (1996). View articlePMID: 8841139

3.The structure and function of the aspartic proteinases. Davies DR. 19, 189-215, (1990). PMID: 2194475

4.The aspartic proteases. Szecsi PB. Scand. J. Clin. Lab. Invest. Suppl. 210, 5-22, (1992). PMID: 1455179

5.Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases. Rao JK, Erickson JW, Wlodawer A. Biochemistry 30, 4663-71, (1991). View articlePMID: 1851433

6.Families of aspartic peptidases, and those of unknown catalytic mechanism. Rawlings ND, Barrett AJ. Meth. Enzymol. 248, 105-20, (1995). View articlePMID: 7674916

7.HIV-1 protease mutations and inhibitor modifications monitored on a series of complexes. Structural basis for the effect of the A71V mutation on the active site. Skalova T, Dohnalek J, Duskova J, Petrokova H, Hradilek M, Soucek M, Konvalinka J, Hasek J. J. Med. Chem. 49, 5777-84, (2006). View articlePMID: 16970402

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