Importance of Potential Interhelical Salt-bridges Involving Interior Residues for Coiled-coil Stability and Quaternary Structure

McClain, Diana L.; Gurnon, Daniel G.; Oakley, Martha G.

doi:10.1016/s0022-2836(02)01072-0

Cited by 40 publications

(34 citation statements)

References 73 publications

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“…Previously elucidated factors include lateral pairing of nonpolar side chains (9-16), which is driven by stereochemical complementarity, and lateral pairing of polar side chains (9)(10)(11)(12)(13)(14)(15)(16)33), which is driven by hydrogen bonding (at least for Asn-Asn pairs). In addition, pairing preferences are influenced by the electrostatic interactions (attractive or repulsive) between ionized side chains (34)(35)(36)(37)(38)(39). Our findings indicate that vertical interactions must be considered as well if we are to understand the origins of dimerization selectivity among natural coiled-coil sequences and expand current abilities to predict and design such interactions.…”

Section: Discussionmentioning

confidence: 85%

Preferred side-chain constellations at antiparallel coiled-coil interfaces

Hadley

Testa

Woolfson

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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Reliable predictive rules that relate protein sequence to structure would facilitate postgenome predictive biology and the engineering and de novo design of peptides and proteins. Through a combination of experiment and analysis of the protein data bank (PDB), we have deciphered and rationalized new rules for helixhelix interfaces of a common protein-folding and association motif, the antiparallel dimeric coiled coil. These interfaces are defined by a specific pattern of interactions among largely hydrophobic side chains often referred to as knobs-into-holes (KIH) packing: a knob from one helix inserts into a hole formed by four residues on the partner. Previous work has focused on lateral interactions within the KIH motif, for example, between an a position on one helix and a d position on the other in an antiparallel coiled coil. We show that vertical interactions within the KIH motif, such as a -a-a , are energetically important as well. The experimental and database analyses concur regarding preferred vertical combinations, which can be rationalized as leading to favorable side-chain interactions that we call constellations. The findings presented here highlight an unanticipated level of complexity in coiled-coil interactions, and our analysis of a few specific constellations illustrates a general, multipronged approach to addressing this complexity.backbone thioester exchange ͉ knobs-into-holes packing ͉ peptides ͉ protein design ͉ protein folding

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Section: Discussionmentioning

confidence: 85%

Preferred side-chain constellations at antiparallel coiled-coil interfaces

Hadley

Testa

Woolfson

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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“…The changes in secondary structure indicated that the structure of the HNE-treated tropomyosin had become more disordered, as based on the calculations performed using the JASCO secondary structure software. According to a previous study (McClain, Gurnon, & Oakley, 2002), this occurs because the amino acid side chains of tropomyosin combine with HNE, disrupting the original van der Waals interactions that maintain the protein's secondary structure and hence rearranging it to a certain degree. Generally, HNE treatment decreases a protein's allergenicity by destroying its epitope conformation.…”

Section: Effect Of Hne Treatment On the Structure Of Shrimp Tropomyosinmentioning

confidence: 99%

Effect of 4-hydroxy-2-nonenal treatment on the IgE binding capacity and structure of shrimp (Metapenaeus ensis) tropomyosin

Lin

Yuan

et al. 2016

Food Chemistry

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“…Two or more ␣-helices supercoil around one another to associate in a parallel or antiparallel orientation. Mutagenesis of apolar residues that are positioned to form a hydrophobic core in the ␣-helix of the heptad repeat (25,26) have been shown to alter ␣-helix conformation. Point mutations for influenza, human immunodeficiency virus (HIV) gp41 or other viral proteins alter ␣-helix formation and disrupt viral-induced membrane fusion (1,4,5,10,15,34,43).…”

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confidence: 99%

The C Terminus of the B5 Receptor for Herpes Simplex Virus Contains a Functional Region Important for Infection

Pérez‐Romero

Fuller

2005

J Virol

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. 79:7419-7430, 2005). Heptad repeats found in the B5 C terminus are predicted to form an ␣-helix for coiled coil structure. We used mutagenesis and synthetic peptides with wild-type and mutant sequences to examine the function of the heptad repeat motif in HSV binding and entry into porcine cells that express B5 and for infection of naturally susceptible human HEp-2 cells. B5 with point mutations predicted to disrupt the putative C-terminal coiled coil failed to mediate HSV binding and entry into porcine cells. Synthetic peptides that contain the single amino acid changes lose the blocking activity of HSV entry. We concluded that the C terminus of B5 contains a functional region that is important for the B5 receptor to mediate events in HSV entry. Structural evidence that this functional region forms coiled coil structures is under investigation. Blocking of HSV interaction with the C-terminal region of the B5 receptor is a new potential target site to intervene in the virus infection of human cells.Herpes simplex virus (HSV) is a prevalent human pathogen that establishes a lifelong infection in its human host. It replicates at the site of entry into the host, most typically to cause oral or genital lesions. Latency is established in neuronal cells from which it reactivates periodically to cause recurrent lesions. The immune system of a healthy person usually can limit lesions to a small localized area. However, HSV causes severe complications and morbidity for immunosuppressed, chronically ill, or bedridden individuals (20,23). Accumulating evidence suggests a possible role for HSV or other infectious agents in the development of neurodegenerative disease (11,12,39).A recently characterized human gene designated human fetal lung cDNA B5 (hfl-B5) (32a) is expressed in a wide range of tissues and encodes a 43-kDa gene product (B5) that mediates HSV entry. Its features differ from the known human receptor proteins for HSV that engage glycoprotein D (gD) (41). The viral ligand for B5 has not yet been determined. The hfl-B5 sequence contains heptad repeats strongly predicted to form coiled coil structure. Coiled coils are composed of leucine zipper motifs that form ␣-helices (16). Two or more ␣-helices supercoil around one another to associate in a parallel or antiparallel orientation. Mutagenesis of apolar residues that are positioned to form a hydrophobic core in the ␣-helix of the heptad repeat (25, 26) have been shown to alter ␣-helix conformation. Point mutations for influenza, human immunodeficiency virus (HIV) gp41 or other viral proteins alter ␣-helix formation and disrupt viral-induced membrane fusion (1,4,5,10,15,34,43). They have been identified as functional features in some cellular and viral fusion proteins (6, 40).Although the mechanisms by which viruses fuse membranes at entry or spread are not yet clear, heptad repeats are a functional part of fusion machinery in a growing number of viral fusion proteins (3,13,28,40). The first characterized of these are hemagglutinin (HA) of influenza virus (34) a...

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Importance of Potential Interhelical Salt-bridges Involving Interior Residues for Coiled-coil Stability and Quaternary Structure

Cited by 40 publications

References 73 publications

Preferred side-chain constellations at antiparallel coiled-coil interfaces

Preferred side-chain constellations at antiparallel coiled-coil interfaces

Effect of 4-hydroxy-2-nonenal treatment on the IgE binding capacity and structure of shrimp (Metapenaeus ensis) tropomyosin

The C Terminus of the B5 Receptor for Herpes Simplex Virus Contains a Functional Region Important for Infection

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