1oby: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1oby]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OBY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OBY FirstGlance]. <br> | <table><tr><td colspan='2'>[[1oby]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OBY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OBY FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nte|1nte]], [[1obx|1obx]], [[1obz|1obz]], [[1ejp|1ejp]], [[1ejq|1ejq]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nte|1nte]], [[1obx|1obx]], [[1obz|1obz]], [[1ejp|1ejp]], [[1ejq|1ejq]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oby OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1oby RCSB], [http://www.ebi.ac.uk/pdbsum/1oby PDBsum]</span></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=1oby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oby OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1oby RCSB], [http://www.ebi.ac.uk/pdbsum/1oby PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/SDC4_HUMAN SDC4_HUMAN]] Cell surface proteoglycan that bears heparan sulfate. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Cooper, D R | [[Category: Cooper, D R]] | ||
[[Category: Derewenda, U | [[Category: Derewenda, U]] | ||
[[Category: Derewenda, Z S | [[Category: Derewenda, Z S]] | ||
[[Category: Devedjiev, Y | [[Category: Devedjiev, Y]] | ||
[[Category: Kang, B S | [[Category: Kang, B S]] | ||
[[Category: Adhesion-complex]] | [[Category: Adhesion-complex]] | ||
[[Category: Cell adhesion]] | [[Category: Cell adhesion]] | ||
Revision as of 15:46, 25 December 2014
CRYSTAL STRUCTURE OF THE COMPLEX OF PDZ2 OF SYNTENIN WITH A SYNDECAN-4 PEPTIDE.CRYSTAL STRUCTURE OF THE COMPLEX OF PDZ2 OF SYNTENIN WITH A SYNDECAN-4 PEPTIDE.
Structural highlights
Function[SDC4_HUMAN] Cell surface proteoglycan that bears heparan sulfate. 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 PubMedCrystal structures of the PDZ2 domain of the scaffolding protein syntenin, both unbound and in complexes with peptides derived from C termini of IL5 receptor (alpha chain) and syndecan, reveal the molecular roots of syntenin's degenerate specificity. Three distinct binding sites (S(0), S(-1), and S(-2)), with affinities for hydrophobic side chains, function in a combinatorial way: S(-1) and S(-2) act together to bind syndecan, while S(0) and S(-1) are involved in the binding of IL5Ralpha. Neither mode of interaction is consistent with the prior classification scheme, which defined the IL5Ralpha interaction as class I (-S/T-X-phi) and the syndecan interaction as class II (-phi-X-phi). These results, in conjunction with other emerging structural data on PDZ domains, call for a revision of their classification and of the existing model of their mechanism. Molecular roots of degenerate specificity in syntenin's PDZ2 domain: reassessment of the PDZ recognition paradigm.,Kang BS, Cooper DR, Devedjiev Y, Derewenda U, Derewenda ZS Structure. 2003 Jul;11(7):845-53. PMID:12842047[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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