1KJG
SUBSTRATE SHAPE DETERMINES SPECIFICITY OF RECOGNITION RECOGNITION FOR HIV-1 PROTEASE: ANALYSIS OF CRYSTAL STRUCTURES OF SIX SUBSTRATE COMPLEXES
Summary for 1KJG
| Entry DOI | 10.2210/pdb1kjg/pdb |
| Related | 1F7A 1KJ4 1KJ7 1KJF 1KJH |
| Descriptor | POL POLYPROTEIN, GAG POLYPROTEIN, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | reverse transcriptase, rnase h, substrate recognition, hydrolase |
| Biological source | Human immunodeficiency virus 1 |
| Cellular location | Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P03369 |
| Total number of polymer chains | 3 |
| Total formula weight | 22748.70 |
| Authors | Schiffer, C.A. (deposition date: 2001-12-04, release date: 2002-03-06, Last modification date: 2023-08-16) |
| Primary citation | Prabu-Jeyabalan, M.,Nalivaika, E.,Schiffer, C.A. Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes. Structure, 10:369-381, 2002 Cited by PubMed Abstract: The homodimeric HIV-1 protease is the target of some of the most effective antiviral AIDS therapy, as it facilitates viral maturation by cleaving ten asymmetric and nonhomologous sequences in the Gag and Pol polyproteins. Since the specificity of this enzyme is not easily determined from the sequences of these cleavage sites alone, we solved the crystal structures of complexes of an inactive variant (D25N) of HIV-1 protease with six peptides that correspond to the natural substrate cleavage sites. When the protease binds to its substrate and buries nearly 1000 A2 of surface area, the symmetry of the protease is broken, yet most internal hydrogen bonds and waters are conserved. However, no substrate side chain hydrogen bond is conserved. Specificity of HIV-1 protease appears to be determined by an asymmetric shape rather than a particular amino acid sequence. PubMed: 12005435DOI: 10.1016/S0969-2126(02)00720-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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