1g1q: Difference between revisions

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-[[Image:1g1q.gif|left|200px]]<br />
-<applet load="1g1q" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1g1q, resolution 2.4&Aring;" />
-'''Crystal structure of P-selectin lectin/EGF domains'''<br />
-==Overview==
+==Crystal structure of P-selectin lectin/EGF domains==
-P-, E- and L-selectin constitute a family of cell adhesion receptors that, mediate the initial tethering and rolling of leukocytes on inflamed, endothelium as a prelude to their firm attachment and extravasation into, tissues. The selectins bind weakly to sialyl Lewisx (SLe(X))-like glycans, but with high-affinity to specific glycoprotein counterreceptors, including PSGL-1. Here, we report crystal structures of human P- and, E-selectin constructs containing the lectin and EGF (LE) domains, co-complexed with SLe(X). We also present the crystal structure of, P-selectin LE co-complexed with the N-terminal domain of human PSGL-1, modified by both tyrosine sulfation and SLe(X). These structures reveal, differences in how E- and P-selectin bind SLe(X) and the molecular basis, of the high-affinity interaction between P-selectin and PSGL-1.
+<StructureSection load='1g1q' size='340' side='right'caption='[[1g1q]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1g1q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G1Q 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]] 2.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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=1g1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1q OCA], [https://pdbe.org/1g1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g1q RCSB], [https://www.ebi.ac.uk/pdbsum/1g1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1q ProSAT]</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/g1/1g1q_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=1g1q ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+P-, E- and L-selectin constitute a family of cell adhesion receptors that mediate the initial tethering and rolling of leukocytes on inflamed endothelium as a prelude to their firm attachment and extravasation into tissues. The selectins bind weakly to sialyl Lewisx (SLe(X))-like glycans, but with high-affinity to specific glycoprotein counterreceptors, including PSGL-1. Here, we report crystal structures of human P- and E-selectin constructs containing the lectin and EGF (LE) domains co-complexed with SLe(X). We also present the crystal structure of P-selectin LE co-complexed with the N-terminal domain of human PSGL-1 modified by both tyrosine sulfation and SLe(X). These structures reveal differences in how E- and P-selectin bind SLe(X) and the molecular basis of the high-affinity interaction between P-selectin and PSGL-1.
-==Disease==
+Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1.,Somers WS, Tang J, Shaw GD, Camphausen RT Cell. 2000 Oct 27;103(3):467-79. PMID:11081633<ref>PMID:11081633</ref>
-Known diseases associated with this structure: Atopy, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173610 173610]], Platelet alpha/delta storage pool deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173610 173610]]
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-G1Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and MRD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G1Q OCA].
+</div>
+<div class="pdbe-citations 1g1q" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1., Somers WS, Tang J, Shaw GD, Camphausen RT, Cell. 2000 Oct 27;103(3):467-79. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11081633 11081633]
+*[[Selectin|Selectin]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Camphausen, R.T.]]
+[[Category: Camphausen RT]]
-[[Category: Somers, W.S.]]
+[[Category: Somers WS]]
-[[Category: CA]]
-[[Category: MRD]]
-[[Category: adhesion molecule]]
-[[Category: egf]]
-[[Category: lectin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:59:31 2007''