1by6: Difference between revisions

Revision as of 19:54, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1by6.png

Template:STRUCTURE 1by6

PEPTIDE OF HUMAN APOLIPOPROTEIN C-IIPEPTIDE OF HUMAN APOLIPOPROTEIN C-II

Template:ABSTRACT PUBMED 10903476

About this StructureAbout this Structure

1BY6 is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

Structure of a biologically active fragment of human serum apolipoprotein C-II in the presence of sodium dodecyl sulfate and dodecylphosphocholine., Storjohann R, Rozek A, Sparrow JT, Cushley RJ, Biochim Biophys Acta. 2000 Jul 19;1486(2-3):253-64. PMID:10903476

Page seeded by OCA on Mon Jun 30 19:54:17 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1by6.jpg|left|200px]]
+{{Seed}}
+[[Image:1by6.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1by6|  PDB=1by6  |  SCENE=  }}
-'''PEPTIDE OF HUMAN APOLIPOPROTEIN C-II'''
+===PEPTIDE OF HUMAN APOLIPOPROTEIN C-II===
-==Overview==
+<!--
-We have studied the three-dimensional structure of a biologically active peptide of apolipoprotein C-II (apoC-II) in the presence of lipid mimetics by CD and NMR spectroscopy. This peptide, corresponding to residues 44-79 of apoC-II, has been shown to reverse the symptoms of genetic apoC-II deficiency in a human subject. A comparison of alpha-proton secondary shifts and CD spectroscopic data indicates that the structure of apoC-II(44-79) is similar in the presence of dodecylphosphocholine and sodium dodecyl sulfate. The three-dimensional structure of apoC-II(44-79) in the presence of sodium dodecyl sulfate, determined by relaxation matrix calculations, contains two amphipathic helical domains formed by residues 50-58 and 67-75, separated by a non-helical linker centered at Tyr63. The C-terminal helix is terminated by a loop formed by residues 76-79. The C-terminal helix is better defined and has a larger hydrophobic face than the N-terminal helix, which leads us to propose that the C-terminal helix together with the non-helical Ile66 constitute the primary lipid binding domain of apoC-II(44-79). Based on our structure we suggest a new mechanism of lipoprotein lipase activation in which both helices of apoC-II(44-79) remain lipid bound, while the seven-residue interhelical linker extends away from the lipid surface in order to project Tyr63 into the apoC-II binding site of lipoprotein lipase.
+The line below this paragraph, {{ABSTRACT_PUBMED_10903476}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10903476 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10903476}}
 ==About this Structure==
-BY6 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY6 OCA].
+BY6 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY6 OCA].
 ==Reference==
@@ Line 29: / Line 33: @@
 [[Category: Lipid association]]
 [[Category: Lpl activation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:06:25 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:54:17 2008''