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== | ==CRYSTAL STRUCTURE OF MOUSE MAJOR URINARY PROTEIN (MUP-I) COMPLEXED WITH HYDROXY-METHYL-HEPTANONE== | ||
<StructureSection load='1i05' size='340' side='right'caption='[[1i05]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1i05]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I05 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=LTL:6-HYDROXY-6-METHYL-HEPTAN-3-ONE'>LTL</scene></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=1i05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i05 OCA], [https://pdbe.org/1i05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i05 RCSB], [https://www.ebi.ac.uk/pdbsum/1i05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i05 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MUP6_MOUSE MUP6_MOUSE] Binds pheromones that are released from drying urine of males. These pheromones affect the sexual behavior of females. | |||
== 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/i0/1i05_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=1i05 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The mouse major urinary proteins are pheromone-binding proteins that function as carriers of volatile effectors of mouse physiology and behavior. Crystal structures of recombinant mouse major urinary protein-I (MUP-I) complexed with the synthetic pheromones, 2-sec-butyl-4,5-dihydrothiazole and 6-hydroxy-6-methyl-3-heptanone, have been determined at high resolution. The purification of MUP-I from mouse liver and a high-resolution structure of the natural isolate are also reported. These results show the binding of 6-hydroxy-6-methyl-3-heptanone to MUP-I, unambiguously define ligand orientations for two pheromones within the MUP-I binding site, and suggest how different chemical classes of pheromones can be accommodated within the MUP-I beta-barrel. | The mouse major urinary proteins are pheromone-binding proteins that function as carriers of volatile effectors of mouse physiology and behavior. Crystal structures of recombinant mouse major urinary protein-I (MUP-I) complexed with the synthetic pheromones, 2-sec-butyl-4,5-dihydrothiazole and 6-hydroxy-6-methyl-3-heptanone, have been determined at high resolution. The purification of MUP-I from mouse liver and a high-resolution structure of the natural isolate are also reported. These results show the binding of 6-hydroxy-6-methyl-3-heptanone to MUP-I, unambiguously define ligand orientations for two pheromones within the MUP-I binding site, and suggest how different chemical classes of pheromones can be accommodated within the MUP-I beta-barrel. | ||
Structural basis of pheromone binding to mouse major urinary protein (MUP-I).,Timm DE, Baker LJ, Mueller H, Zidek L, Novotny MV Protein Sci. 2001 May;10(5):997-1004. PMID:11316880<ref>PMID:11316880</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1i05" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Baker LJ]] | |||
[[Category: Baker | [[Category: Mueller H]] | ||
[[Category: Mueller | [[Category: Novotny MV]] | ||
[[Category: Novotny | [[Category: Timm DE]] | ||
[[Category: Timm | [[Category: Zidek L]] | ||
[[Category: Zidek | |||
Latest revision as of 11:30, 6 November 2024
CRYSTAL STRUCTURE OF MOUSE MAJOR URINARY PROTEIN (MUP-I) COMPLEXED WITH HYDROXY-METHYL-HEPTANONECRYSTAL STRUCTURE OF MOUSE MAJOR URINARY PROTEIN (MUP-I) COMPLEXED WITH HYDROXY-METHYL-HEPTANONE
Structural highlights
FunctionMUP6_MOUSE Binds pheromones that are released from drying urine of males. These pheromones affect the sexual behavior of females. 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 PubMedThe mouse major urinary proteins are pheromone-binding proteins that function as carriers of volatile effectors of mouse physiology and behavior. Crystal structures of recombinant mouse major urinary protein-I (MUP-I) complexed with the synthetic pheromones, 2-sec-butyl-4,5-dihydrothiazole and 6-hydroxy-6-methyl-3-heptanone, have been determined at high resolution. The purification of MUP-I from mouse liver and a high-resolution structure of the natural isolate are also reported. These results show the binding of 6-hydroxy-6-methyl-3-heptanone to MUP-I, unambiguously define ligand orientations for two pheromones within the MUP-I binding site, and suggest how different chemical classes of pheromones can be accommodated within the MUP-I beta-barrel. Structural basis of pheromone binding to mouse major urinary protein (MUP-I).,Timm DE, Baker LJ, Mueller H, Zidek L, Novotny MV Protein Sci. 2001 May;10(5):997-1004. PMID:11316880[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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