1y02: Difference between revisions
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[[Image:1y02.gif|left|200px]] | [[Image:1y02.gif|left|200px]] | ||
'''Crystal Structure of a FYVE-type domain from caspase regulator CARP2''' | {{Structure | ||
|PDB= 1y02 |SIZE=350|CAPTION= <scene name='initialview01'>1y02</scene>, resolution 1.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal Structure of a FYVE-type domain from caspase regulator CARP2''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1Y02 is a [ | 1Y02 is a [[Single protein]] structure of 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=1Y02 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15576038 15576038] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc-binding module]] | [[Category: zinc-binding module]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:16:44 2008'' | ||
Revision as of 13:16, 20 March 2008
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| 1y02, resolution 1.8Å | |||||||||||||
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| Ligands: | ZN | ||||||||||||
| 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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