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1y02

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Revision as of 16:22, 3 November 2021

Crystal Structure of a FYVE-type domain from caspase regulator CARP2

Structural highlights

1y02 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1]

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 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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ McDonald ER 3rd, El-Deiry WS. Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth. Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):6170-5. Epub 2004 Apr 6. PMID:15069192 doi:http://dx.doi.org/10.1073/pnas.0307459101
↑ Tibbetts MD, Shiozaki EN, Gu L, McDonald ER 3rd, El-Deiry WS, Shi Y. Crystal structure of a FYVE-type zinc finger domain from the caspase regulator CARP2. Structure. 2004 Dec;12(12):2257-63. PMID:15576038 doi:10.1016/j.str.2004.10.007

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1y02"

@@ Line 3: / Line 3: @@
 <StructureSection load='1y02' size='340' side='right'caption='[[1y02]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<table><tr><td colspan='2'>[[1y02]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/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>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1y02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y02 OCA], [https://pdbe.org/1y02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y02 RCSB], [https://www.ebi.ac.uk/pdbsum/1y02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y02 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[[https://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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1y02

From Proteopedia

Revision as of 16:22, 3 November 2021

Crystal Structure of a FYVE-type domain from caspase regulator CARP2

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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