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1r0d
From Proteopedia
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HIP1R THATCH DOMAIN CORE
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.
About this Structure
1R0D is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 14:45:39 2008
