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
Line 1: Line 1:
-
[[Image:1lsh.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1lsh.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1lsh| PDB=1lsh | SCENE= }}
{{STRUCTURE_1lsh| PDB=1lsh | SCENE= }}
-
'''LIPID-PROTEIN INTERACTIONS IN LIPOVITELLIN'''
+
===LIPID-PROTEIN INTERACTIONS IN LIPOVITELLIN===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12135361}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12135361 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12135361}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Plasma apolipoprote apolipoprotein b]]
[[Category: Plasma apolipoprote apolipoprotein b]]
[[Category: Vitellogenin]]
[[Category: Vitellogenin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:14:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:02:29 2008''

Revision as of 19:02, 2 July 2008

Image:1lsh.png

Template:STRUCTURE 1lsh

LIPID-PROTEIN INTERACTIONS IN LIPOVITELLIN

Template:ABSTRACT PUBMED 12135361

About this Structure

1LSH is a Protein complex structure of sequences from Ichthyomyzon unicuspis. Full crystallographic information is available from OCA.

Reference

Lipid-protein interactions in lipovitellin., Thompson JR, Banaszak LJ, Biochemistry. 2002 Jul 30;41(30):9398-409. PMID:12135361

Page seeded by OCA on Wed Jul 2 22:02:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lsh"
Personal tools