3lyn
From Proteopedia
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| - | + | ==STRUCTURE OF GREEN ABALONE LYSIN DIMER== | |
| - | === | + | <StructureSection load='3lyn' size='340' side='right' caption='[[3lyn]], [[Resolution|resolution]] 1.70Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3lyn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Haliotis_fulgens Haliotis fulgens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LYN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LYN 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=3lyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lyn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lyn RCSB], [http://www.ebi.ac.uk/pdbsum/3lyn PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ly/3lyn_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Abalone sperm lysin is a 16 kDa acrosomal protein used by sperm to create a hole in the egg vitelline envelope. Lysins from seven California abalone exhibit species-specificity in binding to their egg receptor, and range in sequence identity from 63 % to 90 %. The crystal structure of the sperm lysin dimer from Haliotis fulgens (green abalone) has been determined to 1.71 A by multiple isomorphous replacement. Comparisons with the structure of the lysin dimer from Haliotis rufescens (red abalone) reveal a similar overall fold and conservation of features contributing to lysin's amphipathic character. The two structures do, however, exhibit differences in surface residues and electrostatics. A large clustering of non-conserved surface residues around the waist and clefts of the dimer, and differences in charged residues around these regions, indicate areas of the molecule which may be involved in species-specific egg recognition. | ||
| - | + | The high resolution crystal structure of green abalone sperm lysin: implications for species-specific binding of the egg receptor.,Kresge N, Vacquier VD, Stout CD J Mol Biol. 2000 Mar 10;296(5):1225-34. PMID:10698629<ref>PMID:10698629</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Haliotis fulgens]] | [[Category: Haliotis fulgens]] | ||
| - | [[Category: Kresge, N | + | [[Category: Kresge, N]] |
| - | [[Category: Stout, C D | + | [[Category: Stout, C D]] |
| - | [[Category: Vacquier, V D | + | [[Category: Vacquier, V D]] |
[[Category: Abalone lysin]] | [[Category: Abalone lysin]] | ||
[[Category: Cell adhesion]] | [[Category: Cell adhesion]] | ||
[[Category: Fertilization protein]] | [[Category: Fertilization protein]] | ||
[[Category: Gamete recognition protein]] | [[Category: Gamete recognition protein]] | ||
Revision as of 15:53, 18 December 2014
STRUCTURE OF GREEN ABALONE LYSIN DIMER
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