1bke: Difference between revisions

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[[Image:1bke.gif|left|200px]]<br />

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

<applet load="1bke" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1bke, resolution 3.15Å" />

'''HUMAN SERUM ALBUMIN IN A COMPLEX WITH MYRISTIC ACID AND TRI-IODOBENZOIC ACID'''<br />

==Overview==

Human serum albumin (HSA) is the most abundant protein in the circulatory, system. Its principal function is to transport fatty acids, but it is also, capable of binding a great variety of metabolites and drugs. Despite, intensive efforts, the detailed structural basis of fatty acid binding to, HSA has remained elusive. We have now determined the crystal structure of, HSA complexed with five molecules of myristate at 2.5 A resolution. The, fatty acid molecules bind in long, hydrophobic pockets capped by polar, side chains, many of which are basic. These pockets are distributed, asymmetrically throughout the HSA molecule, despite its symmetrical, repeating domain structure.

Human serum albumin (HSA) is the most abundant protein in the circulatory system. Its principal function is to transport fatty acids, but it is also capable of binding a great variety of metabolites and drugs. Despite intensive efforts, the detailed structural basis of fatty acid binding to HSA has remained elusive. We have now determined the crystal structure of HSA complexed with five molecules of myristate at 2.5 A resolution. The fatty acid molecules bind in long, hydrophobic pockets capped by polar side chains, many of which are basic. These pockets are distributed asymmetrically throughout the HSA molecule, despite its symmetrical repeating domain structure.

==Disease==

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==About this Structure==

1BKE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MYR and B3I as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1BKE OCA].

1BKE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MYR:'>MYR</scene> and <scene name='pdbligand=B3I:'>B3I</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BKE OCA].

==Reference==

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[[Category: plasma protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 16~~:11:~~03 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:56:15 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1bke.gif|left|200px]]<br />
+[[Image:1bke.gif|left|200px]]<br /><applet load="1bke" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1bke" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1bke, resolution 3.15&Aring;" />
 '''HUMAN SERUM ALBUMIN IN A COMPLEX WITH MYRISTIC ACID AND TRI-IODOBENZOIC ACID'''<br />
 ==Overview==
-Human serum albumin (HSA) is the most abundant protein in the circulatory, system. Its principal function is to transport fatty acids, but it is also, capable of binding a great variety of metabolites and drugs. Despite, intensive efforts, the detailed structural basis of fatty acid binding to, HSA has remained elusive. We have now determined the crystal structure of, HSA complexed with five molecules of myristate at 2.5 A resolution. The, fatty acid molecules bind in long, hydrophobic pockets capped by polar, side chains, many of which are basic. These pockets are distributed, asymmetrically throughout the HSA molecule, despite its symmetrical, repeating domain structure.
+Human serum albumin (HSA) is the most abundant protein in the circulatory system. Its principal function is to transport fatty acids, but it is also capable of binding a great variety of metabolites and drugs. Despite intensive efforts, the detailed structural basis of fatty acid binding to HSA has remained elusive. We have now determined the crystal structure of HSA complexed with five molecules of myristate at 2.5 A resolution. The fatty acid molecules bind in long, hydrophobic pockets capped by polar side chains, many of which are basic. These pockets are distributed asymmetrically throughout the HSA molecule, despite its symmetrical repeating domain structure.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-BKE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MYR and B3I as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BKE OCA].
+BKE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MYR:'>MYR</scene> and <scene name='pdbligand=B3I:'>B3I</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BKE OCA].
 ==Reference==
@@ Line 27: / Line 26: @@
 [[Category: plasma protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:11:03 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:56:15 2008''