1qy1

<table><tr><td colspan='2'>[[1qy1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QY1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1QY1 FirstGlance]. <br>

</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PRZ:2-ISOBUTYL-3-METHOXYPYRAZINE'>PRZ</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qy0|1qy0]], [[1qy2|1qy2]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MUP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1qy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qy1 OCA], [http://pdbe.org/1qy1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qy1 RCSB], [http://www.ebi.ac.uk/pdbsum/1qy1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qy1 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/MUP1_MOUSE MUP1_MOUSE]] Binds pheromones that are released from drying urine of males. These pheromones affect the sexual behavior of females.

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== Publication Abstract from PubMed ==

In the present study we examine the thermodynamics of binding of two related pyrazine-derived ligands to the major urinary protein, MUP-I, using a combination of isothermal titration calorimetry (ITC), X-ray crystallography, and NMR backbone (15)N and methyl side-chain (2)H relaxation measurements. Global thermodynamics data derived from ITC indicate that binding is driven by favorable enthalpic contributions, rather than the classical entropy-driven hydrophobic effect. Unfavorable entropic contributions from the protein backbone and side-chain residues in the vicinity of the binding pocket are partially offset by favorable entropic contributions at adjacent positions, suggesting a "conformational relay" mechanism whereby increased rigidity of residues on ligand binding are accompanied by increased conformational freedom of side chains in adjacent positions. The principal driving force governing ligand affinity and specificity can be attributed to solvent-driven enthalpic effects from desolvation of the protein binding pocket.

Thermodynamics of binding of 2-methoxy-3-isopropylpyrazine and 2-methoxy-3-isobutylpyrazine to the major urinary protein.,Bingham RJ, Findlay JB, Hsieh SY, Kalverda AP, Kjellberg A, Perazzolo C, Phillips SE, Seshadri K, Trinh CH, Turnbull WB, Bodenhausen G, Homans SW J Am Chem Soc. 2004 Feb 18;126(6):1675-81. PMID:14871097<ref>PMID:14871097</ref>

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

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<div class="pdbe-citations 1qy1" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Lk3 transgenic mice]]

[[Category: Bingham, R J]]

[[Category: Bodenhausen, G]]

[[Category: Findlay, J B.C]]

[[Category: Homans, S W]]

[[Category: Hsieh, S Y]]

[[Category: Kalverda, A P]]

[[Category: Kjellberg, A]]

[[Category: Perazzolo, C]]

[[Category: Phillips, S E.V]]

[[Category: Seshadri, K]]

[[Category: Trinh, C H]]

[[Category: Turnbull, W B]]

[[Category: Transport protein]]