This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1lsh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1lsh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lsh, resolution 1.90&Aring;" /> '''LIPID-PROTEIN INTERA...)
Current revision (06:06, 3 April 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1lsh.gif|left|200px]]<br /><applet load="1lsh" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1lsh, resolution 1.90&Aring;" />
 
-
'''LIPID-PROTEIN INTERACTIONS IN LIPOVITELLIN'''<br />
 
-
==Overview==
+
==LIPID-PROTEIN INTERACTIONS IN LIPOVITELLIN==
-
The refined molecular structure of lipovitellin is described using, synchrotron cryocrystallographic data to 1.9 A resolution. Lipovitellin is, the predominant lipoprotein found in the yolk of egg-laying animals and is, involved in lipid and metal storage. It is thought to be related in amino, acid sequence to segments of apolipoprotein B and the microsomal transfer, protein responsible for the assembly of low-density lipoproteins., Lipovitellin contains a heterogeneous mixture of about 16% (w/w), noncovalently bound lipid, mostly phospholipid. Previous X-ray structural, studies at ambient temperature described several different protein domains, including a large cavity in each subunit of the dimeric protein. The, cavity was free of any visible electron density for lipid molecules at, room temperature, suggesting that only dynamic interactions exist with the, protein. An important result from this crystallographic study at 100 K is, the appearance of some bound ordered lipid along the walls of the binding, cavity. The precise identification of the lipid type is difficult because, of discontinuities in the electron density. Nonetheless, the conformations, of 7 phospholipids and 43 segments of hydrocarbon chains greater than 5, atoms in length have been discovered. The conformations of the bound lipid, and the interactions between protein and lipid provide insights into the, factors governing lipoprotein formation.
+
<StructureSection load='1lsh' size='340' side='right'caption='[[1lsh]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[1lsh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ichthyomyzon_unicuspis Ichthyomyzon unicuspis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LSH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LSH FirstGlance]. <br>
-
1LSH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Ichthyomyzon_unicuspis Ichthyomyzon unicuspis] with PLD and UPL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LSH OCA].
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-
 
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PLD:DIUNDECYL+PHOSPHATIDYL+CHOLINE'>PLD</scene>, <scene name='pdbligand=UPL:UNKNOWN+BRANCHED+FRAGMENT+OF+PHOSPHOLIPID'>UPL</scene></td></tr>
-
==Reference==
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lsh OCA], [https://pdbe.org/1lsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lsh RCSB], [https://www.ebi.ac.uk/pdbsum/1lsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lsh ProSAT]</span></td></tr>
-
Lipid-protein interactions in lipovitellin., Thompson JR, Banaszak LJ, Biochemistry. 2002 Jul 30;41(30):9398-409. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12135361 12135361]
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/VIT_ICHUN VIT_ICHUN] Precursor of the major egg-yolk proteins that are sources of nutrients during early development of oviparous organisms.
 +
== 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/ls/1lsh_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=1lsh ConSurf].
 +
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
[[Category: Ichthyomyzon unicuspis]]
[[Category: Ichthyomyzon unicuspis]]
-
[[Category: Protein complex]]
+
[[Category: Large Structures]]
-
[[Category: Banaszak, L.J.]]
+
[[Category: Banaszak LJ]]
-
[[Category: Thompson, J.R.]]
+
[[Category: Thompson JR]]
-
[[Category: PLD]]
+
-
[[Category: UPL]]
+
-
[[Category: apob]]
+
-
[[Category: lipoprotein]]
+
-
[[Category: lipovitellin]]
+
-
[[Category: microsomal triglyceride transfer pr boundary lipid]]
+
-
[[Category: phospholipid structure]]
+
-
[[Category: plasma apolipoprote apolipoprotein b]]
+
-
[[Category: vitellogenin]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:50:27 2007''
+

Current revision

LIPID-PROTEIN INTERACTIONS IN LIPOVITELLIN

PDB ID 1lsh

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/1lsh"
Personal tools