Lipocalins – a family portrait

Grzyb, Joanna; Latowski, Dariusz; Strzałka, Kazimierz

doi:10.1016/j.jplph.2005.12.007

Cited by 179 publications

(171 citation statements)

References 148 publications

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“…Low-sequence conservation of cavity residues simply reflects the diverse nature of ligands accomodated by a common architecture. 22,32,42,43,48 In summary, our X-ray crystal structures of MUP-IV elucidate the role of E118 in MUP-IV and reinforce the role of Y120 in ligand binding within the MUP family. In each structure, we observe the carboxyl of E118 (G118 in MUP-I and MUP-II) to form a bifurcated hydrogen bond with the hydroxyl of Y120 and each of the four ligands presented here, replacing the ordered water network observed in MUP-I and MUP-II.…”

Section: Discussionsupporting

confidence: 67%

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High resolution X‐ray structures of mouse major urinary protein nasal isoform in complex with pheromones

et al. 2010

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In mice, the major urinary proteins (MUP) play a key role in pheromonal communication by binding and transporting semiochemicals. MUP-IV is the only isoform known to be expressed in the vomeronasal mucosa. In comparison with the MUP isoforms that are abundantly excreted in the urine, MUP-IV is highly specific for the male mouse pheromone 2-sec-butyl-4,5-dihydrothiazole (SBT). To examine the structural basis of this ligand preference, we determined the X-ray crystal structure of MUP-IV bound to three mouse pheromones: SBT, 2,5-dimethylpyrazine, and 2-heptanone. We also obtained the structure of MUP-IV with 2-ethylhexanol bound in the cavity. These four structures show that relative to the major excreted MUP isoforms, three amino acid substitutions within the binding calyx impact ligand coordination. The F103 for A along with F54 for L result in a smaller cavity, potentially creating a more closely packed environment for the ligand. The E118 for G substitution introduces a charged group into a hydrophobic environment. The sidechain of E118 is observed to hydrogen bond to polar groups on all four ligands with nearly the same geometry as seen for the water-mediated hydrogen bond network in the MUP-I and MUP-II crystal structures. These differences in cavity size and interactions between the protein and ligand are likely to contribute to the observed specificity of MUP-IV.

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Section: Discussionsupporting

confidence: 67%

“…42,43 Lipocalins are currently of medical interest because of the allergic nature of excreted lipocalins from some species, including mouse. 44,45 Lipocalins are also being engineered to target specific molecules for both medical and biotech applications.…”

Section: Discussionmentioning

confidence: 99%

High resolution X‐ray structures of mouse major urinary protein nasal isoform in complex with pheromones

et al. 2010

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“…A1M is a member of the lipocalin protein family, and the recently published crystal structure of human A1M [8] displays the typical lipocalin structural features ( Figure 2). The lipocalins are a group of 40-50 proteins found in all branches of life [9]. They share a common protein fold: a single polypeptide, 150-190 amino acid residues, and forms an antiparallel eight-stranded β-barrel with one closed and one open end.…”

Section: Structurementioning

confidence: 99%

A1M, an extravascular tissue cleaning and housekeeping protein

Åkerström¹,

Gram²

2014

Free Radical Biology and Medicine

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“…Indeed, a DALI (Holm and Sander, 1994) structural similarity search clearly assigns AOC to the lipocalin fold, finding as the top hits retinol binding protein (RBP; 1AQB) and nitrophorin (1NP1) each with a Z-score of 3.2. The lipocalin protein family Brew, 1985, 1987;Grzyb et al, 2006) is a large group of small extracellular proteins with great diversity at the sequence level but mostly with either three characteristic short conserved sequence motifs (SCR I-III; the kernel lipocalins) or else one conserved motif (SCR I; the outlier lipocalins). However, the crystal structures are highly conserved and comprise a single eight-stranded continuously hydrogen-bonded antiparallel b-barrel with an integral ligand binding site ( Figure 5).…”

Section: Structural Comparison With Other Proteinsmentioning

confidence: 99%

The Crystal Structure of Arabidopsis thaliana Allene Oxide Cyclase: Insights into the Oxylipin Cyclization Reaction

2006

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We describe the crystallization and structure elucidation of Arabidopsis thaliana allene oxide cyclase 2 (AOC2), a key enzyme in the biosynthesis of jasmonates. In a coupled reaction with allene oxide synthase, AOC2 releases the first cyclic and biologically active metabolite, 12-oxo-phytodienoic acid (OPDA). AOC2 (AT3G25770) folds into an eight-stranded antiparallel b-barrel with a C-terminal partial helical extension. The protein forms a hydrophobic binding cavity with two distinct polar patches. AOC2 is trimeric in crystals, in vitro and in planta. Based on the observed folding pattern, we assigned AOC2 as a low molecular weight member of the lipocalin family with enzymatic activity in plants. We determined the binding position of the competitive inhibitor vernolic acid (a substrate analog) in the binding pocket. Based on models for bound substrate 12,13-epoxy-9,11,15-octadecatrienoic acid and product OPDA, we propose a reaction scheme that explains the influence of the C15 double bond on reactivity. Reaction is promoted by anchimeric assistance through a conserved Glu residue. The transition state with a pentadienyl carbocation and an oxyanion is stabilized by a strongly bound water molecule and favorable p-p interactions with aromatic residues in the cavity. Stereoselectivity results from steric restrictions to the necessary substrate isomerizations imposed by the protein.

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Lipocalins – a family portrait

Cited by 179 publications

References 148 publications

High resolution X‐ray structures of mouse major urinary protein nasal isoform in complex with pheromones

High resolution X‐ray structures of mouse major urinary protein nasal isoform in complex with pheromones

A1M, an extravascular tissue cleaning and housekeeping protein

The Crystal Structure of Arabidopsis thaliana Allene Oxide Cyclase: Insights into the Oxylipin Cyclization Reaction

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