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Beta-propeller crys...
Beta-propeller crystal structure of Psathyrella velutina lectin: an integrin-like fungal protein interacting with monosaccharides and calcium.
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Cioci, Gianluca (författare)
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Mitchell, Edward P (författare)
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Chazalet, Valerie (författare)
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visa fler...
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Debray, Henri (författare)
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Oscarson, Stefan (författare)
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- Lahmann, Martina, 1963 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry,Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, S-10691 Stokholm, Sweden
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Gautier, Catherine (författare)
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Breton, Christelle (författare)
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Perez, Serge (författare)
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Imberty, Anne (författare)
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(creator_code:org_t)
- Elsevier BV, 2006
- 2006
- Engelska.
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Ingår i: Journal of molecular biology. - : Elsevier BV. - 0022-2836 .- 1089-8638. ; 357:5, s. 1575-91
- Relaterad länk:
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https://gup.ub.gu.se...
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https://doi.org/10.1...
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https://urn.kb.se/re...
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Abstract
Ämnesord
Stäng
- The lectin from the mushroom Psathyrella velutina recognises specifically N-acetylglucosamine and N-acetylneuraminic acid containing glycans. The crystal structure of the 401 amino acid residue lectin shows that it adopts a very regular seven-bladed beta-propeller fold with the N-terminal region tucked into the central cavity around the pseudo 7-fold axis. In the complex with N-acetylglucosamine, six monosaccharides are bound in pockets located between two consecutive propeller blades. Due to the repeats shown by the sequence the binding sites are very similar. Five hydrogen bonds between the protein and the sugar hydroxyl and N-acetyl groups stabilize the complex, together with the hydrophobic interactions with a conserved tyrosine and histidine. The complex with N-acetylneuraminic acid shows molecular mimicry with the same hydrogen bond network, but with different orientations of the carbohydrate ring in the binding site. The beta-hairpin loops connecting the two inner beta-strands of each blade are metal binding sites and two to three calcium ions were located in the structure. The multispecificity and high multivalency of this mushroom lectin, combined with its similarity to the extracellular domain of an important class of cell adhesion molecules, integrins, are another example of the outstanding success of beta-propeller structures as molecular binding machines in nature.
Ämnesord
- NATURVETENSKAP -- Kemi -- Organisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Organic Chemistry (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- Acetylglucosamine
- chemistry
- metabolism
- Agaricales
- chemistry
- Amino Acid Sequence
- Calcium
- metabolism
- Crystallography
- X-Ray
- Fungal Proteins
- chemistry
- genetics
- metabolism
- Hydrogen Bonding
- Integrins
- chemistry
- metabolism
- Lectins
- chemistry
- genetics
- metabolism
- Models
- Molecular
- Molecular Sequence Data
- Monosaccharides
- metabolism
- N-Acetylneuraminic Acid
- metabolism
- Protein Binding
- Protein Conformation
- Protein Folding
- Sequence Alignment
- lectin
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas
- Av författaren/redakt...
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Cioci, Gianluca
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Mitchell, Edward ...
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Chazalet, Valeri ...
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Debray, Henri
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Oscarson, Stefan
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Lahmann, Martina ...
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visa fler...
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Gautier, Catheri ...
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Breton, Christel ...
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Perez, Serge
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Imberty, Anne
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visa färre...
- Om ämnet
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- NATURVETENSKAP
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NATURVETENSKAP
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och Kemi
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och Organisk kemi
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- NATURVETENSKAP
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NATURVETENSKAP
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och Biologi
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och Biokemi och mole ...
- Artiklar i publikationen
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Journal of molec ...
- Av lärosätet
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Göteborgs universitet
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Kungliga Tekniska Högskolan