Refined crystal structure of calcium-liganded carp parvalbumin 4.25 at 1.5-.ANG. resolution

Kumar, Vinod; Lee, Lana; Edwards, Brian F.P.

doi:10.1021/bi00458a010

Cited by 86 publications

(54 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The rCyp c 1.01 structure was generated by homology modeling (30,31) using the crystal structures of a carp parvalbumin with an isoelectric point (pI) of 4.25 (data base entry code P02618) (32) and silver hake parvalbumin (pI of 4.2; data base entry code P56503) (33) as templates. The energyminimized model was prepared with Swissmodel (30,31) and drawn using the programs Molscript (34) and Raster3D (35).…”

Section: Three-dimensional Structural Modelingmentioning

confidence: 99%

Recombinant Carp Parvalbumin, the Major Cross-Reactive Fish Allergen: A Tool for Diagnosis and Therapy of Fish Allergy

Swoboda¹,

Bugajska-Schretter²,

Verdino

et al. 2002

The Journal of Immunology

220

168

View full text Add to dashboard Cite

IgE-mediated reactions to fish allergens represent one of the most frequent causes of food allergy. We have constructed an expression cDNA library from carp (Cyprinus carpio) muscle in phage λgt11 and used serum IgE from a fish allergic patient to isolate 33 cDNA clones that coded for two parvalbumin isoforms (Cyp c 1.01 and Cyp c 1.02) with comparable IgE binding capacities. Both isoforms represented calcium-binding proteins that belonged to the β-lineage of parvalbumins. The Cyp c 1.01 cDNA was overexpressed in Escherichia coli, and rCyp c 1.01 was purified to homogeneity. Circular dichroism analysis and mass spectroscopy showed that rCyp c 1.01 represented a folded protein with mainly α-helical secondary structure and a molecular mass of 11,416 Da, respectively. rCyp c 1.01 reacted with IgE from all fish-allergic patients tested (n = 60), induced specific and dose-dependent basophil histamine release, and contained most of the IgE epitopes (70%) present in natural allergen extracts from cod, tuna, and salmon. Therefore, it may be used to identify patients suffering from IgE-mediated fish allergy. The therapeutic potential of rCyp c 1.01 is indicated by our findings that rabbit Abs raised against rCyp c 1.01 inhibited the binding of IgE (n = 25) in fish-allergic patients to rCyp c 1.01 between 35 and 97% (84% mean inhibition) and that depletion of calcium strongly reduced IgE recognition of rCyp c 1.01. The latter results suggest that it will be possible to develop strategies for immunotherapy for fish allergy that are based on calcium-free hypoallergenic rCyp c 1.01 derivatives.

show abstract

Section: Three-dimensional Structural Modelingmentioning

confidence: 99%

Recombinant Carp Parvalbumin, the Major Cross-Reactive Fish Allergen: A Tool for Diagnosis and Therapy of Fish Allergy

Swoboda¹,

Bugajska-Schretter²,

Verdino

et al. 2002

The Journal of Immunology

220

168

View full text Add to dashboard Cite

show abstract

“…The angles, dihedral angles, and distances defining the geometry of the H-bonds were calculated from protein structures in the PDB-apoCaM: 1QX5 (Schumacher et al 2004), 1CFD , 1DMO (Zhang et al 1995b), holoCaM: 1EXR (Wilson and Brunger 2000), 1J70 and 1J7P (Chou et al 2001), crambin: 1EJG (Jelsch et al 2000), protein G: 1IGD (Derrick and Wigley 1994), ubiquitin: 1UBQ (Vijay- Kumar et al 1987), parvalbumin: 4CPV (Kumar et al 1990), and IFABP: 1IFC (Sacchettini 1989). For structures lacking amide protons, H-bond distances were calculated after protons were added to their respective PDB structures by software (CHARM22), and the NH distance was set to the value observed in the ultra-high-resolution X-ray structure (Jelsch et al 2000) of crambin (1.01 Å ).…”

Section: Parameters Describing H-bond Geometrymentioning

confidence: 99%

Solvent‐induced differentiation of protein backbone hydrogen bonds in calmodulin

et al. 2007

View full text Add to dashboard Cite

In apo and holoCaM, almost half of the hydrogen bonds (H-bonds) at the protein backbone expected from the corresponding NMR or X-ray structures were not detected by h3 J NC9 couplings. The paucity of the h3 J NC9 couplings was considered in terms of dynamic features of these structures. We examined a set of seven proteins and found that protein-backbone H-bonds form two groups according to the h3 J NC9 couplings measured in solution. H-bonds that have h3 J NC9 couplings above the threshold of 0.2 Hz show distance/angle correlation among the H-bond geometrical parameters, and appear to be supported by the backbone dynamics in solution. The other H-bonds have no such correlation; they populate the waterexposed and flexible regions of proteins, including many of the CaM helices. The observed differentiation in a dynamical behavior of backbone H-bonds in apo and holoCaM appears to be related to protein functions.

show abstract

“…An average of the values obtained by these methods was calculated. For the Chen method, the average length of a helical chain (n) was estimated at 12, based on crystallography data for the EF region of carp (PI 4.25) parvalbumin (Kretsinger & Nockolds, 1973;Kumar et al, 1990).…”

Section: Amino Acid Analysismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…X-ray crystallography and NMR data reveal a strong structural homology between members of the parvalbumin subfamily. For example, pike 4.10 and carp 4.25 (Kumar et al, 1990;Declercq et al, 1991), both P-parvalbumins, are very similar in tertiary structure.SHPV-B is a 108-amino acid P-parvalbumin isolated from white muscle of silver hake (Merluccius bilinearis). This approximately 11.4-kDa protein is the major of three isoforms purified from this source (Zhang et al, 1990).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Characterization of a helix‐loop‐helix (EF hand) motif of silver hake parvalbumin isoform B

Revett¹,

Nelson²,

King³

et al. 1997

Protein Science

View full text Add to dashboard Cite

Parvalbumins are a class of calcium-binding proteins characterized by the presence of several helix-loop-helix (EFhand) motifs. It is suspected that these proteins evolved via intragene duplication from a single EF-hand. Silver hake parvalbumin (SHPV) consists of three EF-type helix-loop-helix regions, two of which have the ability to bind calcium. The three helix-loop-helix motifs are designated AB, CD, and EF, respectively. In this study, native silver hake parvalbumin isoform B (SHPV-B) has been sequenced by mass spectrometry. The sequence indicates that this parvalbumin is a P-lineage parvalbumin. SHPV-B was cleaved into two major fragments, consisting of the ABCD and EF regions of the native protein. The 33-amino acid EF fragment (residues 76-108), containing one of the calcium ion binding sites in native SHPV-B, has been isolated and studied for its structural characteristics, ability to bind divalent and trivalent cations, and for its propensity to undergo metal ion-induced self-association. The presence of Ca2+ does not induce significant secondary structure in the EF fragment. However, NMR and CD results indicate significant secondary structure promotion in the EF fragment in the presence of the higher charge-density trivalent cations. Sedimentation equilibrium analysis results show that the EF fragment exists in a monomer-dimer equilibrium when complexed with La'+.Keywords: calcium-binding protein; EF-hand; helix-loop-helix; parvalbumin; silver hake Calcium-binding proteins are a class of proteins with important functions in enzyme activation, muscle contraction, and cell growth. A common structural characteristic of these proteins is the EFhand, a helix-loop-helix motif formed by a sequence of about 30 amino acids (Kretsinger & Nockolds, 1973;Kretsinger, 1975; Kretsinger & Nelson, 1976). Members of this homologous group of proteins contain from two to eight repeats of the helix-loophelix motif, with the EF domains generally occumng in pairs. The fact that EF-hands naturally occur in pairs implies that this domain partnering plays an important role in protein stabilization and function. It is suspected that, through intragene duplication, these proteins evolved from a single approximately 40-amino acid ancestral calcium-binding peptide (Kretsinger, 1972). This intragene duplication likely led to an elongated protein with greater stability and specificity than the ancestral protein. About one-third of the EFhand domains in this superfamily of proteins do not bind calcium (Kawasaki & Kretsinger, 1994).Parvalbumins, a subfamily of EF-hand calcium-binding proteins, have three EF-hand repeats, two of which are paired and Reprint requests to: Donald J. Nelson, Gustaf H. Carlson School of Chemistry, Clark University, Worcester, Massachusetts 01610; e-mail: dnelson@vax.clarku.edu. bind calcium tightly. The N-terminal EF-hand noncalcium-binding domain forms a cap that covers the hydrophobic surface formed by the paired C-terminal calcium-binding domains. Within the parvalbumin subfamily, two distinct p...

show abstract

Refined crystal structure of calcium-liganded carp parvalbumin 4.25 at 1.5-.ANG. resolution

Cited by 86 publications

References 19 publications

Recombinant Carp Parvalbumin, the Major Cross-Reactive Fish Allergen: A Tool for Diagnosis and Therapy of Fish Allergy

Recombinant Carp Parvalbumin, the Major Cross-Reactive Fish Allergen: A Tool for Diagnosis and Therapy of Fish Allergy

Solvent‐induced differentiation of protein backbone hydrogen bonds in calmodulin

Characterization of a helix‐loop‐helix (EF hand) motif of silver hake parvalbumin isoform B

Contact Info

Product

Resources

About