1wz4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:28, 6 December 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Solution Conformation of adr subtype HBV Pre-S2 Epitope==
==Solution Conformation of adr subtype HBV Pre-S2 Epitope==
-
<StructureSection load='1wz4' size='340' side='right'caption='[[1wz4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+
<StructureSection load='1wz4' size='340' side='right'caption='[[1wz4]]' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1wz4]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WZ4 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1wz4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hepatitis_B_virus_ad/Japan/S-179/1988 Hepatitis B virus ad/Japan/S-179/1988]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WZ4 FirstGlance]. <br>
-
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wz4 OCA], [http://pdbe.org/1wz4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wz4 RCSB], [http://www.ebi.ac.uk/pdbsum/1wz4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wz4 ProSAT]</span></td></tr>
+
</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=1wz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wz4 OCA], [https://pdbe.org/1wz4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wz4 RCSB], [https://www.ebi.ac.uk/pdbsum/1wz4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wz4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/HBSAG_HBVC5 HBSAG_HBVC5]] The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assumes fusion between virion membrane and endosomal membrane (Probable). In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein (By similarity). The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid (By similarity).
+
[https://www.uniprot.org/uniprot/HBSAG_HBVC5 HBSAG_HBVC5] The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assumes fusion between virion membrane and endosomal membrane (Probable). In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein (By similarity). The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 21: Line 22:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Hepatitis B virus ad/Japan/S-179/1988]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Chi, S W]]
+
[[Category: Chi SW]]
-
[[Category: Han, K H]]
+
[[Category: Han KH]]
-
[[Category: Gene regulation]]
+
-
[[Category: Helix turn helix]]
+

Current revision

Solution Conformation of adr subtype HBV Pre-S2 Epitope

PDB ID 1wz4

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools