2apd: Difference between revisions

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[[~~Image~~:2apd.~~png|left|200px~~]]

==IS APOLIPOPROTEIN D A MAMMALIAN BILIN-BINDING PROTEIN?==

== 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>

== 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.

~~{{STRUCTURE_2apd| PDB=2apd | SCENE= }}~~

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>

==~~=IS APOLIPOPROTEIN D A MAMMALIAN BILIN~~-~~BINDING PROTEIN?===~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~{{ABSTRACT_PUBMED_2083249}}~~

== References ==

==~~Reference~~==

<~~ref group="xtra">PMID:002083249<~~/~~ref~~><~~references group="xtra"~~/>

__TOC__

</StructureSection>

[[Category: Theoretical Model]]

[[Category: Large Structures]]

[[Category: Boguski, M S]]

[[Category: Peitsch, M C]]

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@@ Line 1: / Line 1: @@
 {{Theoretical_model}}
-[[Image:2apd.png|left|200px]]
+==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.
-{{STRUCTURE_2apd|  PDB=2apd  |  SCENE=  }}
+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>
-===IS APOLIPOPROTEIN D A MAMMALIAN BILIN-BINDING PROTEIN?===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_2083249}}
+<div class="pdbe-citations 2apd" style="background-color:#fffaf0;"></div>
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:002083249</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
+[[Category: Theoretical Model]]
+[[Category: Large Structures]]
 [[Category: Boguski, M S]]
 [[Category: Peitsch, M C]]