1y02 | pdb_00001y02
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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 with ZN as ligand. 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
Page seeded by OCA on Mon Nov 12 20:12:59 2007
