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1pwb

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{{STRUCTURE_1pwb| PDB=1pwb | SCENE= }}
{{STRUCTURE_1pwb| PDB=1pwb | SCENE= }}
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'''High resolution crystal structure of an active recombinant fragment of human lung surfactant protein D with maltose'''
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===High resolution crystal structure of an active recombinant fragment of human lung surfactant protein D with maltose===
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==Overview==
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Lung surfactant protein D (SP-D) can directly interact with carbohydrate residues on pulmonary pathogens and allergens, stimulate immune cells, and manipulate cytokine and chemokine profiles during the immune response in the lungs. Therapeutic administration of rfhSP-D, a recombinant homotrimeric fragment of human SP-D comprising the alpha-helical coiled-coil neck plus three CRDs, protects mice against lung allergy and infection caused by the fungal pathogen Aspergillus fumigatus. The high resolution crystal structures of maltose-bound rfhSP-D to 1.4A, and of rfhSP-D to 1.6A, define the fine detail of the mode and nature of carbohydrate recognition and provide insights into how a small fragment of human SP-D can bind to allergens/antigens or whole pathogens, and at the same time recruit and engage effector cells and molecules of humoral immunity. A previously unreported calcium ion, located on the trimeric axis in a pore at the bottom of the funnel formed by the three CRDs and close to the neck-CRD interface, is coordinated by a triad of glutamate residues which are, to some extent, neutralised by their interactions with a triad of exposed lysine residues in the funnel. The spatial relationship between the neck and the CRDs is maintained internally by these lysine residues, and externally by a glutamine, which forms a pair of hydrogen-bonds within an external cleft at each neck-CRD interface. Structural links between the central pore and the cleft suggest a possible effector mechanism for immune cell surface receptor binding in the presence of bound, extended natural lipopolysaccharide and phospholipid ligands. The structural requirements for such an effector mechanism, involving both the trimeric framework for multivalent ligand binding and recognition sites formed from more than one subunit, are present in both native hSP-D and rfhSP-D, providing a possible explanation for the significant biological activity of rfhSP-D.
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(as it appears on PubMed at http://www.pubmed.gov), where 12888356 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12888356}}
==About this Structure==
==About this Structure==
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[[Category: Carbohydrate recognition domain]]
[[Category: Carbohydrate recognition domain]]
[[Category: Collectin]]
[[Category: Collectin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:33:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:56:27 2008''

Revision as of 11:56, 27 July 2008

Image:1pwb.png

Template:STRUCTURE 1pwb

High resolution crystal structure of an active recombinant fragment of human lung surfactant protein D with maltose

Template:ABSTRACT PUBMED 12888356

About this Structure

1PWB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

High-resolution structural insights into ligand binding and immune cell recognition by human lung surfactant protein D., Shrive AK, Tharia HA, Strong P, Kishore U, Burns I, Rizkallah PJ, Reid KB, Greenhough TJ, J Mol Biol. 2003 Aug 8;331(2):509-23. PMID:12888356

Page seeded by OCA on Sun Jul 27 14:56:27 2008

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