1F7A
HOW DOES A SYMMETRIC DIMER RECOGNIZE AN ASYMMETRIC SUBSTRATE? A SUBSTRATE COMPLEX OF HIV-1 PROTEASE.
Summary for 1F7A
| Entry DOI | 10.2210/pdb1f7a/pdb |
| Descriptor | POL POLYPROTEIN, CA-P2 SUBSTRATE, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | capsid, substrate recognition, hydrolase |
| Biological source | Human immunodeficiency virus 1 More |
| 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 | 23033.12 |
| Authors | Schiffer, C.A. (deposition date: 2000-06-26, release date: 2001-06-27, Last modification date: 2023-08-09) |
| Primary citation | Prabu-Jeyabalan, M.,Nalivaika, E.,Schiffer, C.A. How does a symmetric dimer recognize an asymmetric substrate? A substrate complex of HIV-1 protease. J.Mol.Biol., 301:1207-1220, 2000 Cited by PubMed Abstract: The crystal structure of an actual HIV-1 protease-substrate complex is presented at 2.0 A resolution (R-value of 19.7 % (R(free) 23.3 %)) between an inactive variant (D25N) of HIV-1 protease and a long substrate peptide, Lys-Ala-Arg-Val-Leu-Ala-Glu-Ala-Met-Ser, which covers a full binding epitope of capsid(CA)-p2, cleavage site. The substrate peptide is asymmetric in both size and charge distribution. To accommodate this asymmetry the two protease monomers adopt different conformations burying a total of 1038 A(2) of surface area at the protease-substrate interface. The specificity for the CA-p2 substrate peptide is mainly hydrophobic, as most of the hydrogen bonds are made with the backbone of the peptide substrate. Two water molecules bridge the two monomers through the loops Gly49-Gly52 (Gly49'-Gly52') and Pro79'-Val82' (Pro79-Val82). When other complexes are compared, the mobility of these loops is correlated with the content of the P1 and P1' sites. Interdependence of the conformational changes allows the protease to exhibit its wide range of substrate specificity. PubMed: 10966816DOI: 10.1006/jmbi.2000.4018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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