1m9c
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1m9c.gif|left|200px]] | [[Image:1m9c.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1m9c", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1m9c| PDB=1m9c | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type Complex.''' | '''X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type Complex.''' | ||
| Line 32: | Line 29: | ||
[[Category: Sundquist, W I.]] | [[Category: Sundquist, W I.]] | ||
[[Category: Vajdos, F F.]] | [[Category: Vajdos, F F.]] | ||
| - | [[Category: | + | [[Category: Capsid]] |
| - | [[Category: | + | [[Category: Cyclophilin some]] |
| - | [[Category: | + | [[Category: Hiv-1]] |
| - | [[Category: | + | [[Category: Isomerase]] |
| - | [[Category: | + | [[Category: Rotamase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:47:15 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:47, 2 May 2008
X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type Complex.
Overview
Cyclophilins constitute a ubiquitous protein family whose functions include protein folding, transport and signaling. They possess both sequence-specific binding and proline cis-trans isomerase activities, as exemplified by the interaction between cyclophilin A (CypA) and the HIV-1 CA protein. Here, we report crystal structures of CypA in complex with HIV-1 CA protein variants that bind preferentially with the substrate proline residue in either the cis or the trans conformation. Cis- and trans-Pro substrates are accommodated within the enzyme active site by rearrangement of their N-terminal residues and with minimal distortions in the path of the main chain. CypA Arg55 guanidinium group probably facilitates catalysis by anchoring the substrate proline oxygen and stabilizing sp3 hybridization of the proline nitrogen in the transition state.
About this Structure
1M9C is a Protein complex structure of sequences from Homo sapiens and Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
Reference
Structural insights into the catalytic mechanism of cyclophilin A., Howard BR, Vajdos FF, Li S, Sundquist WI, Hill CP, Nat Struct Biol. 2003 Jun;10(6):475-81. PMID:12730686 Page seeded by OCA on Sat May 3 00:47:15 2008
