1y02

<table><tr><td colspan='2'>[[1y02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y02 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1y02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y02 OCA], [http://pdbe.org/1y02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y02 RCSB], [http://www.ebi.ac.uk/pdbsum/1y02 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y02 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/RFFL_HUMAN RFFL_HUMAN]] Has E3 ubiquitin protein ligase activity. Regulates the levels of CASP8 and CASP10 by targeting them for proteasomal degradation. Has anti-apoptotic activity. May bind phosphatidylinositol phosphates.<ref>PMID:15069192</ref>

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== Publication Abstract from PubMed ==

The caspase-associated ring proteins (CARP1 and CARP2) are distinguished from other caspase regulators by the presence of a FYVE-type zinc finger domain. FYVE-type domains are divided into two known classes: FYVE domains that specifically bind to phosphatidylinositol 3-phosphate in lipid bilayers and FYVE-related domains of undetermined function. Here, we report the crystal structure of the N-terminal region of CARP2 (44-139) including the FYVE-type domain and its associated helical bundle at 1.7 A resolution. The structure reveals a cramped phosphoinositide binding pocket and a blunted membrane insertion loop. These structural features indicate that the domain is not optimized to bind to phosphoinositides or insert into lipid bilayers. The CARP2 FYVE-like domain thus defines a third subfamily of FYVE-type domains that are functionally and structurally distinct. Structural analyses provide insights into the possible function of this unique subfamily of FYVE-type domains.

Crystal structure of a FYVE-type zinc finger domain from the caspase regulator CARP2.,Tibbetts MD, Shiozaki EN, Gu L, McDonald ER 3rd, El-Deiry WS, Shi Y Structure. 2004 Dec;12(12):2257-63. PMID:15576038<ref>PMID:15576038</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 1y02" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Gu, L]]

[[Category: Shi, Y]]

[[Category: Shiozaki, E N]]

[[Category: Tibbetts, M D]]

[[Category: Zinc-binding module]]