1l6n: Difference between revisions

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-[[Image:1l6n.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1l6n", creates the "Structure Box" on the page.
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-{{STRUCTURE_1l6n|  PDB=1l6n  |  SCENE=  }}
-'''STRUCTURE OF THE N-TERMINAL 283-RESIDUE FRAGMENT OF THE HIV-1 GAG POLYPROTEIN'''
+==STRUCTURE OF THE N-TERMINAL 283-RESIDUE FRAGMENT OF THE HIV-1 GAG POLYPROTEIN==
+<StructureSection load='1l6n' size='340' side='right'caption='[[1l6n]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1l6n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L6N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L6N FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1l6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l6n OCA], [https://pdbe.org/1l6n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l6n RCSB], [https://www.ebi.ac.uk/pdbsum/1l6n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l6n ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q72497_9HIV1 Q72497_9HIV1] Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity).  Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).[SAAS:SAAS012344_004_011858]
+== 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/l6/1l6n_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=1l6n ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The capsid protein (CA) of the mature human immunodeficiency virus (HIV) contains an N-terminal beta-hairpin that is essential for formation of the capsid core particle. CA is generated by proteolytic cleavage of the Gag precursor polyprotein during viral maturation. We have determined the NMR structure of a 283-residue N-terminal fragment of immature HIV-1 Gag (Gag(283)), which includes the intact matrix (MA) and N-terminal capsid (CA(N)) domains. The beta-hairpin is unfolded in Gag(283), consistent with the proposal that hairpin formation occurs subsequent to proteolytic cleavage of Gag, triggering capsid assembly. Comparison of the immature and mature CA(N) structures reveals that beta-hairpin formation induces a approximately 2 A displacement of helix 6 and a concomitant displacement of the cyclophylin-A (CypA)-binding loop, suggesting a possible allosteric mechanism for CypA-mediated destabilization of the capsid particle during infectivity.
-==Overview==
+Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein.,Tang C, Ndassa Y, Summers MF Nat Struct Biol. 2002 Jul;9(7):537-43. PMID:12032547<ref>PMID:12032547</ref>
-The capsid protein (CA) of the mature human immunodeficiency virus (HIV) contains an N-terminal beta-hairpin that is essential for formation of the capsid core particle. CA is generated by proteolytic cleavage of the Gag precursor polyprotein during viral maturation. We have determined the NMR structure of a 283-residue N-terminal fragment of immature HIV-1 Gag (Gag(283)), which includes the intact matrix (MA) and N-terminal capsid (CA(N)) domains. The beta-hairpin is unfolded in Gag(283), consistent with the proposal that hairpin formation occurs subsequent to proteolytic cleavage of Gag, triggering capsid assembly. Comparison of the immature and mature CA(N) structures reveals that beta-hairpin formation induces a approximately 2 A displacement of helix 6 and a concomitant displacement of the cyclophylin-A (CypA)-binding loop, suggesting a possible allosteric mechanism for CypA-mediated destabilization of the capsid particle during infectivity.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-L6N 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=1L6N OCA].
+</div>
+<div class="pdbe-citations 1l6n" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein., Tang C, Ndassa Y, Summers MF, Nat Struct Biol. 2002 Jul;9(7):537-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12032547 12032547]
+*[[Gag polyprotein|Gag polyprotein]]
+*[[Gag polyprotein 3D structures|Gag polyprotein 3D structures]]
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Human immunodeficiency virus 1]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Ndassa, Y.]]
+[[Category: Ndassa Y]]
-[[Category: Summers, M F.]]
+[[Category: Summers MF]]
-[[Category: Tang, C.]]
+[[Category: Tang C]]
-[[Category: Capsid]]
-[[Category: Gag]]
-[[Category: Matrix]]
-[[Category: Maturation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:35:51 2008''