2ggu
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2ggu.gif|left|200px]] | [[Image:2ggu.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2ggu", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_2ggu| PDB=2ggu | SCENE= }} | |
| - | | | + | |
| - | | | + | |
| - | }} | + | |
'''crystal structure of the trimeric neck and carbohydrate recognition domain of human surfactant protein D in complex with maltotriose''' | '''crystal structure of the trimeric neck and carbohydrate recognition domain of human surfactant protein D in complex with maltotriose''' | ||
| Line 26: | Line 23: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Head, J F.]] | [[Category: Head, J F.]] | ||
| - | [[Category: | + | [[Category: Protein-carbohydrate ligand complex]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:05:35 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:05, 4 May 2008
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. 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 Sun May 4 05:05:35 2008
