1R0D

HIP1R THATCH DOMAIN CORE

Summary for 1R0D

• Entry DOI: 10.2210/pdb1r0d/pdb
• Descriptor: Huntingtin Interacting Protein 12 (2 entities in total)
• Functional Keywords: endocytosis, actin-binding, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, structural protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, perinuclear region: O75146
• Total number of polymer chains: 8
• Total formula weight: 180876.86

Authors

Brett, T.J.,Fremont, D.H.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2003-09-19, release date: 2004-07-06, Last modification date: 2024-11-13)

Primary citation

Brett, T.J.,Legendre-Guillemin, V.,McPherson, P.S.,Fremont, D.H.
Structural definition of the F-actin-binding THATCH domain from HIP1R
Nat.Struct.Mol.Biol., 13:121-130, 2006

PubMed Abstract: 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.

PubMed: 16415883
DOI: 10.1038/nsmb1043

Experimental method

X-RAY DIFFRACTION (1.9 Å)