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New page: left|200px<br /> <applet load="1ce0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ce0, resolution 2.4Å" /> '''TRIMERIZATION SPECIF... |
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== | ==TRIMERIZATION SPECIFICITY IN HIV-1 GP41: ANALYSIS WITH A GCN4 LEUCINE ZIPPER MODEL== | ||
The envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) | <StructureSection load='1ce0' size='340' side='right'caption='[[1ce0]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ce0]] is a 3 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=1CE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CE0 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ce0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ce0 OCA], [https://pdbe.org/1ce0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ce0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ce0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ce0 ProSAT]</span></td></tr> | |||
</table> | |||
== 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/ce/1ce0_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=1ce0 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) consists of a complex of two noncovalently associated subunits, gp120 and gp41. Formation of gp120/gp41 oligomers is thought to be dependent on a 4-3 hydrophobic (heptad) repeat located in the amino-terminal region of the gp41 molecule. We have investigated the role of this heptad repeat in determining the oligomeric structure of gp41 by introducing its buried core residues into the first (a) and fourth (d) positions of the GCN4 leucine-zipper dimerization domain. The mutant peptides fold into trimeric, helical structures, as shown by circular dichroism and equilibrium sedimentation centrifugation. The 2.4 A resolution crystal structure of one such trimer reveals a parallel three-stranded, alpha-helical coiled coil. Thus, the buried core residues from the gp41 heptad repeat direct trimer formation. We suggest that the conserved amino-terminal heptad repeat within the gp41 ectodomain possesses trimerization specificity. | |||
Trimerization specificity in HIV-1 gp41: analysis with a GCN4 leucine zipper model.,Shu W, Ji H, Lu M Biochemistry. 1999 Apr 27;38(17):5378-85. PMID:10220324<ref>PMID:10220324</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1ce0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human immunodeficiency virus 1]] | [[Category: Human immunodeficiency virus 1]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Ji | [[Category: Ji H]] | ||
[[Category: Lu | [[Category: Lu M]] | ||
[[Category: Shu | [[Category: Shu W]] | ||
Latest revision as of 08:50, 9 August 2023
TRIMERIZATION SPECIFICITY IN HIV-1 GP41: ANALYSIS WITH A GCN4 LEUCINE ZIPPER MODELTRIMERIZATION SPECIFICITY IN HIV-1 GP41: ANALYSIS WITH A GCN4 LEUCINE ZIPPER MODEL
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) consists of a complex of two noncovalently associated subunits, gp120 and gp41. Formation of gp120/gp41 oligomers is thought to be dependent on a 4-3 hydrophobic (heptad) repeat located in the amino-terminal region of the gp41 molecule. We have investigated the role of this heptad repeat in determining the oligomeric structure of gp41 by introducing its buried core residues into the first (a) and fourth (d) positions of the GCN4 leucine-zipper dimerization domain. The mutant peptides fold into trimeric, helical structures, as shown by circular dichroism and equilibrium sedimentation centrifugation. The 2.4 A resolution crystal structure of one such trimer reveals a parallel three-stranded, alpha-helical coiled coil. Thus, the buried core residues from the gp41 heptad repeat direct trimer formation. We suggest that the conserved amino-terminal heptad repeat within the gp41 ectodomain possesses trimerization specificity. Trimerization specificity in HIV-1 gp41: analysis with a GCN4 leucine zipper model.,Shu W, Ji H, Lu M Biochemistry. 1999 Apr 27;38(17):5378-85. PMID:10220324[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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