Fel d 1: Difference between revisions
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== '''Structure''' == | == '''Structure''' == | ||
Fel d 1 is a tetrameric glycoprotein of 35 to 39 kDa, by size exclusion chromatography, formed by two identical heterodimers of about 18 kDa, noncovalently linked. These heterodimers are totally α-helical, formed by 8 helices, H1-H4 and H5-H8, corresponding to the 2 and 1 chains, respectively<ref name="[1]"/><ref name="[4]">GRÖNLUND H, Saarne T, Gafvelin G, van Hage M: The Major Cat Allergen, Fel d 1, in Diagnosis and Therapy. Int Arch Allergy Immunol 2010;151:265-274. doi: 10.1159/000250435.</ref>. Chains 1 and 2 are two antiparallel polypeptides, linked via 3 interchain disulfide bonds, formed between cysteine residues at positions Cys3-Cys73, Cys44-Cys48, and Cys70-Cys7, at chains 1 and 2, respectively <ref name="[1]"/><ref name="[4]"/>. Chain 1 has about 8kDa, composed of a residue of 70 amino acids and chain 2 has about 10 kDa, which can be composed of a residue of 90 amino acids, found preferably in the sebaceous glands, or composed of a residue of 92 amino acids, which is expressed by the salivary glands. Its glycan portion is found in chain 2 and the recombinant structure of Fel d 1 reveals that the N33 residue is located in the loop connecting the H2 and H3 helices and that the side chain is exposed to the solvent<ref name="[1]"/><ref name="[4]"/>. | Fel d 1 is a tetrameric [https://en.wikipedia.org/wiki/Glycoprotein glycoprotein] of 35 to 39 kDa, by size exclusion chromatography, formed by two identical heterodimers of about 18 kDa, noncovalently linked. These heterodimers are totally α-helical, formed by 8 helices, H1-H4 and H5-H8, corresponding to the 2 and 1 chains, respectively<ref name="[1]"/><ref name="[4]">GRÖNLUND H, Saarne T, Gafvelin G, van Hage M: The Major Cat Allergen, Fel d 1, in Diagnosis and Therapy. Int Arch Allergy Immunol 2010;151:265-274. doi: 10.1159/000250435.</ref>. Chains 1 and 2 are two antiparallel polypeptides, linked via 3 interchain disulfide bonds, formed between cysteine residues at positions Cys3-Cys73, Cys44-Cys48, and Cys70-Cys7, at chains 1 and 2, respectively <ref name="[1]"/><ref name="[4]"/>. Chain 1 has about 8kDa, composed of a residue of 70 amino acids and chain 2 has about 10 kDa, which can be composed of a residue of 90 amino acids, found preferably in the sebaceous glands, or composed of a residue of 92 amino acids, which is expressed by the salivary glands. Its glycan portion is found in chain 2 and the recombinant structure of Fel d 1 reveals that the N33 residue is located in the loop connecting the H2 and H3 helices and that the side chain is exposed to the solvent<ref name="[1]"/><ref name="[4]"/>. | ||
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In the 3D scene it is possible to <scene name="/12/3456/Sample/1">color</scene> by group | In the 3D scene of the asymmetric unit of Fel d 1 it is possible to <scene name="/12/3456/Sample/1">color</scene> by group, make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein Fel d 1 and visualize four MPD molecules (used in the crystallization of Fel d 1) <ref name="[1]"/> <ref>DOI 10.1002/ijch.201300024</ref> <ref>PMID:21638687</ref>. | ||
=='''Treatment'''== | =='''Treatment'''== | ||