1y02: Difference between revisions

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[[Image:1y02.~~gif~~|left|200px]]

[[Image:1y02.png|left|200px]]

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

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

~~==Overview==~~

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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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_15576038}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15576038 is the PubMed ID number.

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==About this Structure==

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[[Category: Phosphoinositide binding]]

[[Category: Zinc-binding module]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 15~~:43:13 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:32:56 2008''

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-[[Image:1y02.gif|left|200px]]
+{{Seed}}
+[[Image:1y02.png|left|200px]]
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 {{STRUCTURE_1y02|  PDB=1y02  |  SCENE=  }}
-'''Crystal Structure of a FYVE-type domain from caspase regulator CARP2'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15576038}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15576038 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15576038}}
 ==About this Structure==
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 [[Category: Phosphoinositide binding]]
 [[Category: Zinc-binding module]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 15:43:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:32:56 2008''