This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1r0d
From Proteopedia
|
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 Mon Nov 12 18:58:11 2007
