1spp: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1spp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SPP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SPP FirstGlance]. <br> | <table><tr><td colspan='2'>[[1spp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SPP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SPP FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1spp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1spp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1spp RCSB], [http://www.ebi.ac.uk/pdbsum/1spp PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1spp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1spp OCA], [http://pdbe.org/1spp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1spp RCSB], [http://www.ebi.ac.uk/pdbsum/1spp PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1spp" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 05:57, 10 September 2015
THE CRYSTAL STRUCTURES OF TWO MEMBERS OF THE SPERMADHESIN FAMILY REVEAL THE FOLDING OF THE CUB DOMAINTHE CRYSTAL STRUCTURES OF TWO MEMBERS OF THE SPERMADHESIN FAMILY REVEAL THE FOLDING OF THE CUB DOMAIN
Structural highlights
Function[PSP1_PIG] Not yet identified, major porcine seminal plasma protein. Can bind soybean trypsin inhibitor after deglycosylation. 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 PubMedSpermadhesins, 12,000-14,000 M(r) mammalian proteins, include lectins involved in sperm-egg binding and display a single CUB domain architecture. We report the crystal structures of porcine seminal plasma PSP-I/PSP-II, a heterodimer of two glycosylated spermadhesins, and bovine aSFP at 2.4 A and 1.9 A resolution respectively. The crystal structures of two spermadhesins reveal the CUB domain fold.,Romero A, Romao MJ, Varela PF, Kolln I, Dias JM, Carvalho AL, Sanz L, Topfer-Petersen E, Calvete JJ Nat Struct Biol. 1997 Oct;4(10):783-8. PMID:9334740[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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