1y02
From Proteopedia
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 Page seeded by OCA on Sat May 3 15:43:13 2008
