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1y02
From Proteopedia
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|PDB= 1y02 |SIZE=350|CAPTION= <scene name='initialview01'>1y02</scene>, resolution 1.8Å | |PDB= 1y02 |SIZE=350|CAPTION= <scene name='initialview01'>1y02</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<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://www.ebi.ac.uk/pdbsum/1y02 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1y02 RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Shiozaki, E N.]] | [[Category: Shiozaki, E N.]] | ||
[[Category: Tibbetts, M D.]] | [[Category: Tibbetts, M D.]] | ||
| - | [[Category: ZN]] | ||
[[Category: carp2]] | [[Category: carp2]] | ||
[[Category: caspase regulation]] | [[Category: caspase regulation]] | ||
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[[Category: zinc-binding module]] | [[Category: zinc-binding module]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:57:04 2008'' |
Revision as of 21:57, 30 March 2008
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| , resolution 1.8Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of a FYVE-type domain from caspase regulator CARP2
Overview
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.
About this Structure
1Y02 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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