1ypr: Difference between revisions

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 <StructureSection load='1ypr' size='340' side='right'caption='[[1ypr]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ypr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YPR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ypr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YPR FirstGlance]. <br>
-</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=1ypr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ypr OCA], [https://pdbe.org/1ypr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ypr RCSB], [https://www.ebi.ac.uk/pdbsum/1ypr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ypr ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=1ypr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ypr OCA], [https://pdbe.org/1ypr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ypr RCSB], [https://www.ebi.ac.uk/pdbsum/1ypr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ypr ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/PROF_YEAST PROF_YEAST]] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
+[https://www.uniprot.org/uniprot/PROF_YEAST PROF_YEAST] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=1ypr ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The structure of profilin from the budding yeast Saccharomyces cerevisiae has been determined by X-ray crystallography at 2.3 A resolution. The overall fold of yeast profilin is similar to the fold observed for other profilin structures. The interactions of yeast and human platelet profilins with rabbit skeletal muscle actin were characterized by titration microcalorimetry, fluorescence titrations, and nucleotide exchange kinetics. The affinity of yeast profilin for rabbit actin (2.9 microM) is approximately 30-fold weaker than the affinity of human platelet profilin for rabbit actin (0.1 microM), and the relative contributions of entropic and enthalpic terms to the overall free energy of binding are different for the two profilins. The titration of pyrene-labeled rabbit skeletal actin with human profilin yielded a Kd of 2.8 microM, similar to the Kd of 2.0 microM for the interaction between yeast profilin and pyrene-labeled yeast actin. The binding data are discussed in the context of the known crystal structures of profilin and actin, and the residues present at the actin-profilin interface. The affinity of yeast profilin for poly-L-proline was determined from fluorescence measurements and is similar to the reported affinity of Acanthamoeba profilin for poly-L-proline. Yeast profilin was shown to catalyze adenine nucleotide exchange from yeast actin almost 2 orders of magnitude less efficiently than human profilin and rabbit skeletal muscle actin. The in vivo and in vitro properties of yeast profilin mutants with altered poly-L-proline and actin binding sites are discussed in the context of the crystal structure.
-Structure determination and characterization of Saccharomyces cerevisiae profilin.,Eads JC, Mahoney NM, Vorobiev S, Bresnick AR, Wen KK, Rubenstein PA, Haarer BK, Almo SC Biochemistry. 1998 Aug 11;37(32):11171-81. PMID:9698363<ref>PMID:9698363</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1ypr" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Profilin 3D Structures|Profilin 3D Structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
 [[Category: Large Structures]]
-[[Category: Almo, S C]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Eads, J C]]
+[[Category: Almo SC]]
-[[Category: Mahoney, N M]]
+[[Category: Eads JC]]
-[[Category: Actin-binding protein]]
+[[Category: Mahoney NM]]
-[[Category: Cytoskeleton]]
-[[Category: Profilin]]