2g69

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:26, 14 February 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2g69.gif|left|200px]]
 
-
{{Structure
+
==Structure of Unliganded HIV-1 Protease F53L Mutant==
-
|PDB= 2g69 |SIZE=350|CAPTION= <scene name='initialview01'>2g69</scene>, resolution 1.35&Aring;
+
<StructureSection load='2g69' size='340' side='right'caption='[[2g69]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<table><tr><td colspan='2'>[[2g69]] is a 1 chain structure with sequence from [https://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=2G69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G69 FirstGlance]. <br>
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/HIV-1_retropepsin HIV-1 retropepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.16 3.4.23.16] </span>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35&#8491;</td></tr>
-
|GENE=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2g69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g69 OCA], [https://pdbe.org/2g69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g69 RCSB], [https://www.ebi.ac.uk/pdbsum/2g69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g69 ProSAT]</span></td></tr>
-
|DOMAIN=
+
</table>
-
|RELATEDENTRY=
+
== Function ==
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g69 OCA], [http://www.ebi.ac.uk/pdbsum/2g69 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2g69 RCSB]</span>
+
[https://www.uniprot.org/uniprot/Q7SSI0_9HIV1 Q7SSI0_9HIV1]
-
}}
+
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g6/2g69_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2g69 ConSurf].
 +
<div style="clear:both"></div>
-
'''Structure of Unliganded HIV-1 Protease F53L Mutant'''
+
==See Also==
-
 
+
*[[Immunodeficiency virus protease 3D structures|Immunodeficiency virus protease 3D structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
Mutations in HIV-1 protease (PR) that produce resistance to antiviral PR inhibitors are a major problem in AIDS therapy. The mutation F53L arising from antiretroviral therapy was introduced into the flexible flap region of the wild-type PR to study its effect and potential role in developing drug resistance. Compared to wild-type PR, PR(F53L) showed lower (15%) catalytic efficiency, 20-fold weaker inhibition by the clinical drug indinavir, and reduced dimer stability, while the inhibition constants of two peptide analog inhibitors were slightly lower than those for PR. The crystal structure of PR(F53L) was determined in the unliganded form at 1.35 Angstrom resolution in space group P4(1)2(1)2. The tips of the flaps in PR(F53L) had a wider separation than in unliganded wild-type PR, probably due to the absence of hydrophobic interactions of the side-chains of Phe53 and Ile50'. The changes in interactions between the flaps agreed with the reduced stability of PR(F53L) relative to wild-type PR. The altered flap interactions in the unliganded form of PR(F53L) suggest a distinct mechanism for drug resistance, which has not been observed in other common drug-resistant mutants.
+
-
 
+
-
==About this Structure==
+
-
2G69 is a [[Single protein]] structure of sequence from [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=2G69 OCA].
+
-
 
+
-
==Reference==
+
-
Mechanism of drug resistance revealed by the crystal structure of the unliganded HIV-1 protease with F53L mutation., Liu F, Kovalevsky AY, Louis JM, Boross PI, Wang YF, Harrison RW, Weber IT, J Mol Biol. 2006 May 19;358(5):1191-9. Epub 2006 Mar 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16569415 16569415]
+
-
[[Category: HIV-1 retropepsin]]
+
[[Category: Human immunodeficiency virus 1]]
[[Category: Human immunodeficiency virus 1]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Kovalevsky, A Y.]]
+
[[Category: Kovalevsky AY]]
-
[[Category: Liu, F.]]
+
[[Category: Liu F]]
-
[[Category: aspartic protease]]
+
-
[[Category: catalysis]]
+
-
[[Category: flap mutant]]
+
-
[[Category: non-active site mutant]]
+
-
[[Category: unliganded]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:12:23 2008''
+

Current revision

Structure of Unliganded HIV-1 Protease F53L Mutant

PDB ID 2g69

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2g69"
Personal tools