2apd: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(9 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Theoretical Model'''
{{Theoretical_model}}


The entry 2APD is a Theoretical Model titled 'IS APOLIPOPROTEIN D A MAMMALIAN BILIN-BINDING PROTEIN?'.
==IS APOLIPOPROTEIN D A MAMMALIAN BILIN-BINDING PROTEIN?==
<StructureSection load='2apd' size='340' side='right'caption='[[2apd]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2APD FirstGlance]. <br>
</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=2apd FirstGlance], [https://www.ebi.ac.uk/pdbsum/2apd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2apd ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human apolipoprotein D (APO-D) is a serum glycoprotein that has no sequence similarity with other apolipoproteins but rather belongs to the alpha 2-microglobulin superfamily whose other members transport small hydrophobic ligands in a wide variety of biological contexts. To investigate the ligand specificity of APO-D, we analyzed its relationship with the other members of this superfamily and constructed a detailed molecular model using the atomic coordinates of its most closely related homolog--insecticyanin from the tobacco hornworm, Manduca sexta. We studied the geometry of the binding pocket of APO-D and the topology of characteristic patches of both hydrophobic and polar side chains that also occur in crystal structures of insecticyanin and bilin-binding protein from the butterfly Pieris brassicae. From the data obtained we hypothesize that heme-related compounds may be more favorable ligands for APO-D than either cholesterol or cholesteryl ester. Preliminary experiments showed that purified human APO-D binds bilirubin in an approximately one-to-one molar ratio. These results suggest a new biological role for APO-D that is more congruent with its tissue distribution and evolutionary history.


[[Category:Theoretical Model]]
Is apolipoprotein D a mammalian bilin-binding protein?,Peitsch MC, Boguski MS New Biol. 1990 Feb;2(2):197-206. PMID:2083249<ref>PMID:2083249</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 30 09:55:36 2008''
</div>
<div class="pdbe-citations 2apd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Theoretical Model]]
[[Category: Large Structures]]
[[Category: Boguski, M S]]
[[Category: Peitsch, M C]]
Retrieved from "https://proteopedia.org/2apd"