1r13: Difference between revisions

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[[Image:1r13.gif|left|200px]]<br /><applet load="1r13" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1r13.gif|left|200px]]<br /><applet load="1r13" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1r13, resolution 2.1Å" />

'''Carbohydrate recognition and neck domains of surfactant protein A (SP-A)'''<br />

==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.

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==

1R13 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 CA, SO4 and MES as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1R13 OCA].

1R13 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=CA:'>CA</scene>, <scene name='pdbligand=SO4:'>SO4</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=1R13 OCA].

==Reference==

Line 13:

[[Category: Rattus norvegicus]]

[[Category: Single protein]]

[[Category: Head, J.F.]]

[[Category: Head, J F.]]

[[Category: McCormack, F.X.]]

[[Category: McCormack, F X.]]

[[Category: Mealy, T.R.]]

[[Category: Mealy, T R.]]

[[Category: Seaton, B.A.]]

[[Category: Seaton, B A.]]

[[Category: CA]]

[[Category: MES]]

Line 23:

[[Category: crd]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:51 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1r13.gif|left|200px]]<br /><applet load="1r13" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1r13.gif|left|200px]]<br /><applet load="1r13" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1r13, resolution 2.1&Aring;" />
 '''Carbohydrate recognition and neck domains of surfactant protein A (SP-A)'''<br />
 ==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.
+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==
-R13 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 CA, SO4 and MES as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R13 OCA].
+R13 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=CA:'>CA</scene>, <scene name='pdbligand=SO4:'>SO4</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=1R13 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Rattus norvegicus]]
 [[Category: Single protein]]
-[[Category: Head, J.F.]]
+[[Category: Head, J F.]]
-[[Category: McCormack, F.X.]]
+[[Category: McCormack, F X.]]
-[[Category: Mealy, T.R.]]
+[[Category: Mealy, T R.]]
-[[Category: Seaton, B.A.]]
+[[Category: Seaton, B A.]]
 [[Category: CA]]
 [[Category: MES]]
@@ Line 23: / Line 23: @@
 [[Category: crd]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:11:00 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:51 2008''