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1y02

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(New page: 200px<br /> <applet load="1y02" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y02, resolution 1.8&Aring;" /> '''Crystal Structure of...)
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'''Crystal Structure of a FYVE-type domain from caspase regulator CARP2'''<br />
'''Crystal Structure of a FYVE-type domain from caspase regulator CARP2'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1Y02 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y02 OCA].
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1Y02 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y02 OCA].
==Reference==
==Reference==
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[[Category: Gu, L.]]
[[Category: Gu, L.]]
[[Category: Shi, Y.]]
[[Category: Shi, Y.]]
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[[Category: Shiozaki, E.N.]]
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[[Category: Shiozaki, E N.]]
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[[Category: Tibbetts, M.D.]]
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[[Category: Tibbetts, M D.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: carp2]]
[[Category: carp2]]
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[[Category: zinc-binding module]]
[[Category: zinc-binding module]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:12:59 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:00:27 2008''

Revision as of 14:00, 21 February 2008


1y02, resolution 1.8Å

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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 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

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