1r14: Difference between revisions

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{{STRUCTURE_1r14|  PDB=1r14  |  SCENE=  }}  
{{STRUCTURE_1r14|  PDB=1r14  |  SCENE=  }}  


'''Carbohydrate recognition and neck domains of surfactant protein A (Sp-A) containing samarium'''
===Carbohydrate recognition and neck domains of surfactant protein A (Sp-A) containing samarium===




==Overview==
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Surfactant protein A (SP-A), one of four proteins associated with pulmonary surfactant, binds with high affinity to alveolar phospholipid membranes, positioning the protein at the first line of defense against inhaled pathogens. SP-A exhibits both calcium-dependent carbohydrate binding, a characteristic of the collectin family, and specific interactions with lipid membrane components. The crystal structure of the trimeric carbohydrate recognition domain and neck domain of SP-A was solved to 2.1-A resolution with multiwavelength anomalous dispersion phasing from samarium. Two metal binding sites were identified, one in the highly conserved lectin site and the other 8.5 A away. The interdomain carbohydrate recognition domain-neck angle is significantly less in SP-A than in the homologous collectins, surfactant protein D, and mannose-binding protein. This conformational difference may endow the SP-A trimer with a more extensive hydrophobic surface capable of binding lipophilic membrane components. The appearance of this surface suggests a putative binding region for membrane-derived SP-A ligands such as phosphatidylcholine and lipid A, the endotoxic lipid component of bacterial lipopolysaccharide that mediates the potentially lethal effects of Gram-negative bacterial infection.
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{{ABSTRACT_PUBMED_12913002}}


==About this Structure==
==About this Structure==
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[[Category: Alpha helical neck region]]
[[Category: Alpha helical neck region]]
[[Category: Crd]]
[[Category: Crd]]
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