1h8p: Difference between revisions
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<StructureSection load='1h8p' size='340' side='right'caption='[[1h8p]], [[Resolution|resolution]] 1.82Å' scene=''> | <StructureSection load='1h8p' size='340' side='right'caption='[[1h8p]], [[Resolution|resolution]] 1.82Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1h8p]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1h8p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H8P FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PC:PHOSPHOCHOLINE'>PC</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PC:PHOSPHOCHOLINE'>PC</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pdc|1pdc]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pdc|1pdc]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h8p OCA], [https://pdbe.org/1h8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h8p RCSB], [https://www.ebi.ac.uk/pdbsum/1h8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h8p ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/SFP1_BOVIN SFP1_BOVIN]] Could enhance the fertilizing capacity of bull spermatozoa upon interaction with heparin-like glycosaminoglycans present in the female genital tract. Exhibits both simulatory and inhibitory actions on the release of pituitary gonadotropins. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 08:48, 28 April 2021
Bull seminal plasma PDC-109 fibronectin type II moduleBull seminal plasma PDC-109 fibronectin type II module
Structural highlights
Function[SFP1_BOVIN] Could enhance the fertilizing capacity of bull spermatozoa upon interaction with heparin-like glycosaminoglycans present in the female genital tract. Exhibits both simulatory and inhibitory actions on the release of pituitary gonadotropins. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBovine seminal plasma PDC-109 binds to sperm surface choline lipids and promotes sperm capacitation by stimulating the efflux of cholesterol and phospholipids. The structure of PDC-109 with bound phosphorylcholine was solved using MAD data of a single platinum site. Its two globular (40 x 50 x 20 A(3)) Fn2 domains are linked and clustered by a short polypeptide. The choline binding sites lie at the same face of the molecule. Phosphorylcholine binds to the Fn2 domains through a cation-pi interaction between the quaternary ammonium group and a core tryptophan, plus hydrogen bonding between hydroxyls of exposed tyrosines and the phosphate group. The structure of the PDC-109-oPC complex provides a structural ground for the sperm membrane-coating mechanism underlying PDC-109-induced capacitation. Sperm coating mechanism from the 1.8 A crystal structure of PDC-109-phosphorylcholine complex.,Wah DA, Fernandez-Tornero C, Sanz L, Romero A, Calvete JJ Structure. 2002 Apr;10(4):505-14. PMID:11937055[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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