1t7s

<StructureSection load='1t7s' size='340' side='right' caption='[[1t7s]], [[Resolution|resolution]] 2.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[1t7s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T7S FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hx1|1hx1]], [[1i6z|1i6z]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Bag-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans])</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=1t7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1t7s RCSB], [http://www.ebi.ac.uk/pdbsum/1t7s PDBsum], [http://www.topsan.org/Proteins/SECSG/1t7s TOPSAN]</span></td></tr>

[[http://www.uniprot.org/uniprot/BAG1_CAEEL BAG1_CAEEL]] May inhibit the chaperone activity of HSP70/HSC70 by promoting substrate release in an ATP-dependent manner (By similarity).

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t7/1t7s_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Binding of the BAG domain to the eukaryotic chaperone heat-shock protein (Hsp70) promotes ATP-dependent release of the protein substrate from Hsp70. Although the murine and human BAG domains have been shown to form an antiparallel three-helix bundle, the Caenorhabditis elegans BAG domain is formed by two antiparallel helices, while the third helix is extended away and stabilized by crystal-packing interactions. A small beta-sheet between helices 2 and 3 interferes with formation of the intramolecular three-helix bundle. However, intermolecular three-helix bundles are observed throughout the crystal packing and suggest that stable functional dimers and tetramers can be formed in solution. The structure may represent a new folding type of the BAG domain.

Structural genomics of Caenorhabditis elegans: structure of the BAG domain.,Symersky J, Zhang Y, Schormann N, Li S, Bunzel R, Pruett P, Luan CH, Luo M Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1606-10. Epub 2004, Aug 26. PMID:15333932<ref>PMID:15333932</ref>

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

</div>

*[[BAG protein|BAG protein]]

[[Category: Bunzel, R]]

[[Category: Li, S]]

[[Category: Luan, C H]]

[[Category: Luo, M]]

[[Category: Pruett, P]]

[[Category: Structural genomic]]

[[Category: Schormann, N]]

[[Category: Symersky, J]]

[[Category: Zhang, Y]]

[[Category: Secsg]]