2bph: Difference between revisions

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'''STRUCTURE OF MURINE DECTIN-1'''

==Overview==

The murine molecule dectin-1 (known as the beta-glucan receptor in humans) is an immune cell surface receptor implicated in the immunological defense against fungal pathogens. Sequence analysis has indicated that the dectin-1 extracellular domain is a C-type lectin-like domain, and functional studies have established that it binds fungal beta-glucans. We report several dectin-1 crystal structures, including a high-resolution structure and a 2.8 angstroms resolution structure in which a short soaked natural beta-glucan is trapped in the crystal lattice. In vitro characterization of dectin-1 in the presence of its natural ligand indicates higher-order complex formation between dectin-1 and beta-glucans. These combined structural and biophysical data considerably extend the current knowledge of dectin-1 structure and function, and suggest potential mechanisms of defense against fungal pathogens.

==About this Structure==

2BPH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BPH OCA].

==Reference==

Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function., Brown J, O'Callaghan CA, Marshall AS, Gilbert RJ, Siebold C, Gordon S, Brown GD, Jones EY, Protein Sci. 2007 Jun;16(6):1042-52. Epub 2007 May 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17473009 17473009]

[[Category: Mus musculus]]

[[Category: Single protein]]

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[[Category: Fungal recognition]]

[[Category: Receptor]]

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@@ Line 11: / Line 11: @@
 '''STRUCTURE OF MURINE DECTIN-1'''
+==Overview==
+The murine molecule dectin-1 (known as the beta-glucan receptor in humans) is an immune cell surface receptor implicated in the immunological defense against fungal pathogens. Sequence analysis has indicated that the dectin-1 extracellular domain is a C-type lectin-like domain, and functional studies have established that it binds fungal beta-glucans. We report several dectin-1 crystal structures, including a high-resolution structure and a 2.8 angstroms resolution structure in which a short soaked natural beta-glucan is trapped in the crystal lattice. In vitro characterization of dectin-1 in the presence of its natural ligand indicates higher-order complex formation between dectin-1 and beta-glucans. These combined structural and biophysical data considerably extend the current knowledge of dectin-1 structure and function, and suggest potential mechanisms of defense against fungal pathogens.
 ==About this Structure==
 BPH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BPH OCA].
+==Reference==
+Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function., Brown J, O'Callaghan CA, Marshall AS, Gilbert RJ, Siebold C, Gordon S, Brown GD, Jones EY, Protein Sci. 2007 Jun;16(6):1042-52. Epub 2007 May 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17473009 17473009]
 [[Category: Mus musculus]]
 [[Category: Single protein]]
@@ Line 31: / Line 37: @@
 [[Category: Fungal recognition]]
 [[Category: Receptor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:36:56 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 22:20:32 2008''