1r0d

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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