1r14
From Proteopedia
(New page: 200px<br /><applet load="1r14" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r14, resolution 2.5Å" /> '''Carbohydrate recognit...) |
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| - | [[Image:1r14.jpg|left|200px]]<br /><applet load="1r14" size=" | + | [[Image:1r14.jpg|left|200px]]<br /><applet load="1r14" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r14, resolution 2.5Å" /> | caption="1r14, resolution 2.5Å" /> | ||
'''Carbohydrate recognition and neck domains of surfactant protein A (Sp-A) containing samarium'''<br /> | '''Carbohydrate recognition and neck domains of surfactant protein A (Sp-A) containing samarium'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Surfactant protein A (SP-A), one of four proteins associated with | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1R14 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with SM and MES as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1R14 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=SM:'>SM</scene> and <scene name='pdbligand=MES:'>MES</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R14 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Head, J | + | [[Category: Head, J F.]] |
| - | [[Category: McCormack, F | + | [[Category: McCormack, F X.]] |
| - | [[Category: Mealy, T | + | [[Category: Mealy, T R.]] |
| - | [[Category: Seaton, B | + | [[Category: Seaton, B A.]] |
[[Category: MES]] | [[Category: MES]] | ||
[[Category: SM]] | [[Category: SM]] | ||
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[[Category: crd]] | [[Category: crd]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:51 2008'' |
Revision as of 12:45, 21 February 2008
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Carbohydrate recognition and neck domains of surfactant protein A (Sp-A) containing samarium
Overview
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.
About this Structure
1R14 is a Single protein structure of sequence from Rattus norvegicus with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of trimeric carbohydrate recognition and neck domains of surfactant protein A., Head JF, Mealy TR, McCormack FX, Seaton BA, J Biol Chem. 2003 Oct 31;278(44):43254-60. Epub 2003 Aug 11. PMID:12913002
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