1r0d: Difference between revisions

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New page: left|200px<br /> <applet load="1r0d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r0d, resolution 1.90Å" /> '''HIP1R THATCH DOMAIN...
 
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[[Image:1r0d.gif|left|200px]]<br />
[[Image:1r0d.gif|left|200px]]<br /><applet load="1r0d" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1r0d" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1r0d, resolution 1.90&Aring;" />
caption="1r0d, resolution 1.90&Aring;" />
'''HIP1R THATCH DOMAIN CORE'''<br />
'''HIP1R THATCH DOMAIN CORE'''<br />


==Overview==
==Overview==
Huntingtin-interacting protein-1 related (HIP1R) has a crucial, protein-trafficking role, mediating associations between actin and, clathrin-coated structures at the plasma membrane and trans-Golgi network., Here, we characterize the F-actin-binding region of HIP1R, termed the, talin-HIP1/R/Sla2p actin-tethering C-terminal homology (THATCH) domain., The 1.9-A crystal structure of the human HIP1R THATCH core reveals a large, sequence-conserved surface patch created primarily by residues from the, third and fourth helices of a unique five-helix bundle. Point mutations of, seven contiguous patch residues produced significant decreases in F-actin, binding. We also show that THATCH domains have a conserved C-terminal, latch capable of oligomerizing the core, thereby modulating F-actin, engagement. Collectively, these results establish a framework for, investigating the links between endocytosis and actin dynamics mediated by, THATCH domain-containing proteins.
Huntingtin-interacting protein-1 related (HIP1R) has a crucial protein-trafficking role, mediating associations between actin and clathrin-coated structures at the plasma membrane and trans-Golgi network. Here, we characterize the F-actin-binding region of HIP1R, termed the talin-HIP1/R/Sla2p actin-tethering C-terminal homology (THATCH) domain. The 1.9-A crystal structure of the human HIP1R THATCH core reveals a large sequence-conserved surface patch created primarily by residues from the third and fourth helices of a unique five-helix bundle. Point mutations of seven contiguous patch residues produced significant decreases in F-actin binding. We also show that THATCH domains have a conserved C-terminal latch capable of oligomerizing the core, thereby modulating F-actin engagement. Collectively, these results establish a framework for investigating the links between endocytosis and actin dynamics mediated by THATCH domain-containing proteins.


==About this Structure==
==About this Structure==
1R0D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R0D OCA].  
1R0D is a [http://en.wikipedia.org/wiki/Single_protein 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=1R0D OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Brett, T.J.]]
[[Category: Brett, T J.]]
[[Category: Fremont, D.H.]]
[[Category: Fremont, D H.]]
[[Category: MCSG, Midwest.Center.for.Structural.Genomics.]]
[[Category: MCSG, Midwest Center for Structural Genomics.]]
[[Category: actin-binding]]
[[Category: actin-binding]]
[[Category: endocytosis]]
[[Category: endocytosis]]
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[[Category: structural genomics]]
[[Category: structural genomics]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:39 2008''

Revision as of 15:45, 21 February 2008

File:1r0d.gif


1r0d, resolution 1.90Å

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HIP1R THATCH DOMAIN CORE

OverviewOverview

Huntingtin-interacting protein-1 related (HIP1R) has a crucial protein-trafficking role, mediating associations between actin and clathrin-coated structures at the plasma membrane and trans-Golgi network. Here, we characterize the F-actin-binding region of HIP1R, termed the talin-HIP1/R/Sla2p actin-tethering C-terminal homology (THATCH) domain. The 1.9-A crystal structure of the human HIP1R THATCH core reveals a large sequence-conserved surface patch created primarily by residues from the third and fourth helices of a unique five-helix bundle. Point mutations of seven contiguous patch residues produced significant decreases in F-actin binding. We also show that THATCH domains have a conserved C-terminal latch capable of oligomerizing the core, thereby modulating F-actin engagement. Collectively, these results establish a framework for investigating the links between endocytosis and actin dynamics mediated by THATCH domain-containing proteins.

About this StructureAbout this Structure

1R0D is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural definition of the F-actin-binding THATCH domain from HIP1R., Brett TJ, Legendre-Guillemin V, McPherson PS, Fremont DH, Nat Struct Mol Biol. 2006 Feb;13(2):121-30. Epub 2006 Jan 15. PMID:16415883

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