1msb
From Proteopedia
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|PDB= 1msb |SIZE=350|CAPTION= <scene name='initialview01'>1msb</scene>, resolution 2.3Å | |PDB= 1msb |SIZE=350|CAPTION= <scene name='initialview01'>1msb</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HO:HOLMIUM ATOM'>HO</scene> | + | |LIGAND= <scene name='pdbligand=HO:HOLMIUM+ATOM'>HO</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1msb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1msb OCA], [http://www.ebi.ac.uk/pdbsum/1msb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1msb RCSB]</span> | ||
}} | }} | ||
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[[Category: Hendrickson, W A.]] | [[Category: Hendrickson, W A.]] | ||
[[Category: Weis, W I.]] | [[Category: Weis, W I.]] | ||
| - | [[Category: HO]] | ||
[[Category: hepatic lectin]] | [[Category: hepatic lectin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:20:30 2008'' |
Revision as of 19:20, 30 March 2008
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| , resolution 2.3Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE CALCIUM-DEPENDENT LECTIN DOMAIN FROM A RAT MANNOSE-BINDING PROTEIN DETERMINED BY MAD PHASING
Overview
Calcium-dependent (C-type) animal lectins participate in many cell surface recognition events mediated by protein-carbohydrate interactions. The C-type lectin family includes cell adhesion molecules, endocytic receptors, and extracellular matrix proteins. Mammalian mannose-binding proteins are C-type lectins that function in antibody-independent host defense against pathogens. The crystal structure of the carbohydrate-recognition domain of a rat mannose-binding protein, determined as the holmium-substituted complex by multiwavelength anomalous dispersion (MAD) phasing, reveals an unusual fold consisting of two distinct regions, one of which contains extensive nonregular secondary structure stabilized by two holmium ions. The structure explains the conservation of 32 residues in all C-type carbohydrate-recognition domains, suggesting that the fold seen here is common to these domains. The strong anomalous scattering observed at the Ho LIII edge demonstrates that traditional heavy atom complexes will be generally amenable to the MAD phasing method.
About this Structure
1MSB is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing., Weis WI, Kahn R, Fourme R, Drickamer K, Hendrickson WA, Science. 1991 Dec 13;254(5038):1608-15. PMID:1721241
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