1r0d
HIP1R THATCH DOMAIN COREHIP1R THATCH DOMAIN CORE
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHuntingtin-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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