1m9c
From Proteopedia
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| - | [[Image:1m9c.gif|left|200px]] | + | [[Image:1m9c.gif|left|200px]] |
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| - | '''X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type Complex.''' | + | {{Structure |
| + | |PDB= 1m9c |SIZE=350|CAPTION= <scene name='initialview01'>1m9c</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type Complex.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1M9C is a [ | + | 1M9C is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M9C OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12730686 12730686] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Human immunodeficiency virus 1]] | [[Category: Human immunodeficiency virus 1]] | ||
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[[Category: Vajdos, F F.]] | [[Category: Vajdos, F F.]] | ||
[[Category: capsid]] | [[Category: capsid]] | ||
| - | [[Category: cyclophilin | + | [[Category: cyclophilin some]] |
[[Category: hiv-1]] | [[Category: hiv-1]] | ||
[[Category: isomerase]] | [[Category: isomerase]] | ||
[[Category: rotamase]] | [[Category: rotamase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:40:34 2008'' |
Revision as of 10:40, 20 March 2008
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| , resolution 2.00Å | |||||||
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| Activity: | Peptidylprolyl isomerase, with EC number 5.2.1.8 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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