2ggu
From Proteopedia
(New page: 200px<br /> <applet load="2ggu" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ggu, resolution 1.900Å" /> '''crystal structure ...) |
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| - | [[Image:2ggu.gif|left|200px]]<br /> | + | [[Image:2ggu.gif|left|200px]]<br /><applet load="2ggu" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2ggu" size=" | + | |
caption="2ggu, resolution 1.900Å" /> | caption="2ggu, resolution 1.900Å" /> | ||
'''crystal structure of the trimeric neck and carbohydrate recognition domain of human surfactant protein D in complex with maltotriose'''<br /> | '''crystal structure of the trimeric neck and carbohydrate recognition domain of human surfactant protein D in complex with maltotriose'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Surfactant protein D (SP-D) is an innate immune effector that contributes | + | Surfactant protein D (SP-D) is an innate immune effector that contributes to antimicrobial host defense and immune regulation. Interactions of SP-D with microorganisms and organic antigens involve binding of glycoconjugates to the C-type lectin carbohydrate recognition domain (CRD). A trimeric fusion protein encoding the human neck+CRD bound to the aromatic glycoside p-nitrophenyl-alpha-D-maltoside with nearly a log-fold higher affinity than maltose, the prototypical competitor. Maltotriose, which has the same linkage pattern as the maltoside, bound with intermediate affinity. Site-directed substitution of leucine for phenylalanine 335 (Phe-335) decreased affinities for the maltoside and maltotriose without significantly altering the affinity for maltose or glucose, and substitution of tyrosine or tryptophan for leucine restored preferential binding to maltotriose and the maltoside. A mutant with alanine at this position failed to bind to mannan or maltose-substituted solid supports. Crystallographic analysis of the human neck+CRD complexed with maltotriose or p-nitrophenyl-maltoside showed stacking of the terminal glucose or nitrophenyl ring with the aromatic ring of Phe-335. Our studies indicate that Phe-335, which is evolutionarily conserved in all known SP-Ds, plays important, if not critical, roles in SP-D function. |
==About this Structure== | ==About this Structure== | ||
| - | 2GGU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and MLR as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2GGU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MLR:'>MLR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GGU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Head, J | + | [[Category: Head, J F.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: MLR]] | [[Category: MLR]] | ||
[[Category: protein-carbohydrate ligand complex]] | [[Category: protein-carbohydrate ligand complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:31:35 2008'' |
Revision as of 15:31, 21 February 2008
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crystal structure of the trimeric neck and carbohydrate recognition domain of human surfactant protein D in complex with maltotriose
Overview
Surfactant protein D (SP-D) is an innate immune effector that contributes to antimicrobial host defense and immune regulation. Interactions of SP-D with microorganisms and organic antigens involve binding of glycoconjugates to the C-type lectin carbohydrate recognition domain (CRD). A trimeric fusion protein encoding the human neck+CRD bound to the aromatic glycoside p-nitrophenyl-alpha-D-maltoside with nearly a log-fold higher affinity than maltose, the prototypical competitor. Maltotriose, which has the same linkage pattern as the maltoside, bound with intermediate affinity. Site-directed substitution of leucine for phenylalanine 335 (Phe-335) decreased affinities for the maltoside and maltotriose without significantly altering the affinity for maltose or glucose, and substitution of tyrosine or tryptophan for leucine restored preferential binding to maltotriose and the maltoside. A mutant with alanine at this position failed to bind to mannan or maltose-substituted solid supports. Crystallographic analysis of the human neck+CRD complexed with maltotriose or p-nitrophenyl-maltoside showed stacking of the terminal glucose or nitrophenyl ring with the aromatic ring of Phe-335. Our studies indicate that Phe-335, which is evolutionarily conserved in all known SP-Ds, plays important, if not critical, roles in SP-D function.
About this Structure
2GGU is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Contributions of phenylalanine 335 to ligand recognition by human surfactant protein D: ring interactions with SP-D ligands., Crouch E, McDonald B, Smith K, Cafarella T, Seaton B, Head J, J Biol Chem. 2006 Jun 30;281(26):18008-14. Epub 2006 Apr 24. PMID:16636058
Page seeded by OCA on Thu Feb 21 17:31:35 2008
