One type of gamma-turn, rather than the other gives rise to chain-reversal in proteins

Milner‐White, E. James; Ross, Brian M.; Ismail, Rainah; Belhadj-Mostefa, Khaled; Poet, Ron

doi:10.1016/0022-2836(88)90368-3

Cited by 173 publications

(108 citation statements)

References 15 publications

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“…Use of site-specific indices (15) to locate the most probable position for an a-helix containing seven amides yields residues 149-156 with Gly-149 and Ala-156 as N-cap and C-cap residues, respectively. The hydrophobic moments of these postulated a-helices are all (except LP) -87% of values expected for highly amphiphilic surface-seeking a-helices (16 Dihedral angles within the predicted a-helices, P-strands, and inverse yturns were restrained to within 100 of average values (24)(25)(26), and the first and fourth a carbons of each predicted p-turn were restrained to a distance of4-7 A. Each model was subjected to energy minimiztion, followed by molecular dynamics at 900 K, saving one structure every 2.5 ps until 20 structures were generated.…”

Section: Methodsmentioning

confidence: 99%

Circular dichroism, molecular modeling, and serology indicate that the structural basis of antigenic variation in foot-and-mouth disease virus is alpha-helix formation.

France

Piatti

Newman

et al. 1994

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

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Section: Methodsmentioning

confidence: 99%

Circular dichroism, molecular modeling, and serology indicate that the structural basis of antigenic variation in foot-and-mouth disease virus is alpha-helix formation.

France

Piatti

Newman

et al. 1994

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

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“…Inverse ␥-turns are weak, as defined by hydrogen bonding criteria (53), and rarely occur within ␤-hairpins. Although sometimes found at key position in proteins, these weak ␥-turns have been suggested to function as intermediate conformers that stabilize ␤-strands before formation of ␤-sheets (54,55).…”

Section: Overall Structure Of Gpib␣-a1 and Comparison To Unliganded Gmentioning

confidence: 99%

Crystal Structure of the Wild-type von Willebrand Factor A1-Glycoprotein Ibα Complex Reveals Conformation Differences with a Complex Bearing von Willebrand Disease Mutations

Dumas¹,

Kumar²,

McDonagh³

et al. 2004

Journal of Biological Chemistry

186

237

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The adhesion of platelets to the subendothelium of blood vessels at sites of vascular injury under high shear conditions is mediated by a direct interaction between the platelet receptor glycoprotein Ib␣ (GpIb␣) and the A1 domain of the von Willebrand factor (VWF). Here we report the 2.6-Å crystal structure of a complex comprised of the extracellular domain of GpIb␣ and the wild-type A1 domain of VWF. A direct comparison of this structure to a GpIb␣-A1 complex containing "gain-offunction" mutations, A1-R543Q and GpIb␣-M239V, reveals specific structural differences between these complexes at sites near the two GpIb␣-A1 binding interfaces. At the smaller interface, differences in interaction show that the ␣1-␤2 loop of A1 serves as a conformational switch, alternating between an open ␣1-␤2 isomer that allows faster dissociation of GpIb␣-A1, as observed in the wild-type complex, and an extended isomer that favors tight association as seen in the complex containing A1 with a type 2B von Willebrand Disease (VWD) mutation associated with spontaneous binding to GpIb␣. At the larger interface, differences in interaction associated with the GpIb␣-M239V platelet-type VWD mutation are minor and localized but feature discrete ␥-turn conformers at the loop end of the ␤-hairpin structure. The ␤-hairpin, stabilized by a strong classic ␥-turn as seen in the mutant complex, relates to the increased affinity of A1 binding, and the ␤-hairpin with a weak inverse ␥-turn observed in the wild-type complex corresponds to the lower affinity state of GpIb␣. These findings provide important details that add to our understanding of how both type 2B and platelet-type VWD mutations affect GpIb␣-A1 binding affinity.

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“…Figure 4 schematically illustrates three common turn structures which facilitate polypeptide chain reversal in all a-residue sequences (Rose et al 1985). The C 7 or g-turn conformation is generated by the formation of a single seven-atom intramolecularly hydrogen-bonded ring and is characterized by the torsion angles fzK708, jzC708 or f zC708, jzK708 at residue iC1 (Mathews 1972;Milner-White & Poet 1986, 1987Milner-White et al 1988). The C 7 structure is effectively determined by the conformational preferences at a single residue.…”

Section: Introductionmentioning

confidence: 99%

Expanding the polypeptide backbone: hydrogen-bonded conformations in hybrid polypeptides containing the higher homologues of α-amino acids

Chatterjee

Roy

Balaram

2007

J. R. Soc. Interface.

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Half a century has passed since the hydrogen-bonded secondary structures of polypeptides and proteins were first recognized. An extraordinary wealth of conformational information is now available on peptides and proteins, which are formed of a-amino acid residues. More recently, the discovery of well-folded structures in oligopeptides containing b-amino acids has focused a great deal of current interest on the conformational properties of peptides constructed from higher homologues (u) of a-amino acids. This review examines the nature of intramolecularly hydrogen-bonded conformations of hybrid peptides formed by amino acid residues, with a varying number of backbone atoms. The b-turn, a ubiquitous structural feature formed by two residue (aa) segments in proteins and peptides, is stabilized by a 10-atom (C 10 ) intramolecular 4/1 hydrogen bond. Hybrid turns may be classified by comparison with their aa counterparts. The available crystallographic information on hydrogen-bonded hybrid turns is surveyed in this review. Several recent examples demonstrate that individual u-amino acid residues and hybrid dipeptide segments may be incorporated into the regular structures of a-peptides. Examples of both peptide helices and hairpins are presented. The present review explores the relationships between folded conformations in hybrid sequences and their counterparts in all a-residue sequences. The use of stereochemically constrained u-residues promises to expand the range of peptide design strategies to include u-amino acids. This approach is exemplified by well-folded structures like the C 12 (ag) and C 14 (gg) helices formed in short peptides containing multiply substituted g-residues. The achiral g-residue gabapentin is a readily accessible building block in the design of peptides containing g-amino acids. The construction of globular polypeptide structures using diverse hybrid sequences appears to be a realistic possibility.

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One type of gamma-turn, rather than the other gives rise to chain-reversal in proteins

Cited by 173 publications

References 15 publications

Circular dichroism, molecular modeling, and serology indicate that the structural basis of antigenic variation in foot-and-mouth disease virus is alpha-helix formation.

Circular dichroism, molecular modeling, and serology indicate that the structural basis of antigenic variation in foot-and-mouth disease virus is alpha-helix formation.

Crystal Structure of the Wild-type von Willebrand Factor A1-Glycoprotein Ibα Complex Reveals Conformation Differences with a Complex Bearing von Willebrand Disease Mutations

Expanding the polypeptide backbone: hydrogen-bonded conformations in hybrid polypeptides containing the higher homologues of α-amino acids

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