The helix bundle: A reversible lipid binding motif
نویسندگان
چکیده
منابع مشابه
A molecular trigger of lipid binding-induced opening of a helix bundle exchangeable apolipoprotein.
Apolipophorin III (apoLp-III) from the sphinx moth, Manduca sexta, is a helix bundle protein that interacts reversibly with lipoproteins. Its five elongated amphipathic alpha-helices are organized in an antiparallel fashion, with helices 3 and 4 connected by a short 6-residue (PDVEKE) linker helix, termed helix 3'. Upon interaction with lipoproteins, apoLp-III opens to expose a continuous hydro...
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A three dimensional model of the basic Helix-Loop-Helix motif and its sequence specific recognition of DNA is described. The basic-helix I is modeled as a continuous ?-helix because no ?-helix breaking residue is found between the basic region and the first helix. When the basic region of the two peptide monomers are aligned in the successive major groove of the cognate DNA, the hydrophobi...
متن کاملHTHquery: a method for detecting DNA-binding proteins with a helix-turn-helix structural motif
SUMMARY HTHquery is a web-based service to determine if a protein structure has a helix-turn-helix structural motif which could bind to DNA. It is based on a similarity with a set of structural templates, the accessibility of a putative structural motif and a positive electrostatic potential in the neighbourhood of the putative motif. A set of scores are computed, based on each template, using ...
متن کاملRoquin binding to target mRNAs involves a winged helix-turn-helix motif.
Roquin proteins mediate mRNA deadenylation by recognizing a conserved class of stem-loop RNA degradation motifs via their Roquin domain. Here we present the crystal structure of a Roquin domain, revealing a mostly helical protein fold bearing a winged helix-turn-helix motif. By combining structural, biochemical and mutation analyses, we gain insight into the mode of RNA binding. We show that th...
متن کاملThe helix-turn-helix motif of bacterial insertion sequence IS911 transposase is required for DNA binding.
The transposase of IS911, a member of the IS3 family of bacterial insertion sequences, is composed of a catalytic domain located at its C-terminal end and a DNA binding domain located at its N-terminal end. Analysis of the transposases of over 60 members of the IS3 family revealed the presence of a helix-turn-helix (HTH) motif within the N-terminal region. Alignment of these potential secondary...
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ژورنال
عنوان ژورنال: Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology
سال: 2010
ISSN: 1095-6433
DOI: 10.1016/j.cbpa.2009.09.009