1ath: Difference between revisions

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

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

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

caption="1ath, resolution 3.2Å" />

'''THE INTACT AND CLEAVED HUMAN ANTITHROMBIN III COMPLEX AS A MODEL FOR SERPIN-PROTEINASE INTERACTIONS'''<br />

==Overview==

Antithrombin is a member of the serine proteinase inhibitor (serpin), family which contain a flexible reactive site loop that interacts with, and is cleaved by the target proteinase. In cleaved and latent serpins, the reactive site loop is inserted into a large central beta-sheet in the, same molecule, whereas in ovalbumin, a nonfunctional serpin, the reactive, site loop is completely exposed and in an alpha-helical conformation., However, in neither conformation can the reactive site loop bind to target, proteinases. Here we report the structure of an intact and cleaved human, antithrombin complex. The intact reactive site loop is in a novel, conformation that seems well suited for interaction with proteinases such, as thrombin and blood coagulation factor Xa.

Antithrombin is a member of the serine proteinase inhibitor (serpin) family which contain a flexible reactive site loop that interacts with, and is cleaved by the target proteinase. In cleaved and latent serpins, the reactive site loop is inserted into a large central beta-sheet in the same molecule, whereas in ovalbumin, a nonfunctional serpin, the reactive site loop is completely exposed and in an alpha-helical conformation. However, in neither conformation can the reactive site loop bind to target proteinases. Here we report the structure of an intact and cleaved human antithrombin complex. The intact reactive site loop is in a novel conformation that seems well suited for interaction with proteinases such as thrombin and blood coagulation factor Xa.

==About this Structure==

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

1ATH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ATH OCA].

==Reference==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Hol, W.G.J.]]

[[Category: Hol, W G.J.]]

[[Category: Schreuder, H.A.]]

[[Category: Schreuder, H A.]]

[[Category: human antithrombin-iii]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 16~~:01:~~32 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:05 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1ath.gif|left|200px]]<br />
+[[Image:1ath.gif|left|200px]]<br /><applet load="1ath" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1ath" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1ath, resolution 3.2&Aring;" />
 '''THE INTACT AND CLEAVED HUMAN ANTITHROMBIN III COMPLEX AS A MODEL FOR SERPIN-PROTEINASE INTERACTIONS'''<br />
 ==Overview==
-Antithrombin is a member of the serine proteinase inhibitor (serpin), family which contain a flexible reactive site loop that interacts with, and is cleaved by the target proteinase. In cleaved and latent serpins, the reactive site loop is inserted into a large central beta-sheet in the, same molecule, whereas in ovalbumin, a nonfunctional serpin, the reactive, site loop is completely exposed and in an alpha-helical conformation., However, in neither conformation can the reactive site loop bind to target, proteinases. Here we report the structure of an intact and cleaved human, antithrombin complex. The intact reactive site loop is in a novel, conformation that seems well suited for interaction with proteinases such, as thrombin and blood coagulation factor Xa.
+Antithrombin is a member of the serine proteinase inhibitor (serpin) family which contain a flexible reactive site loop that interacts with, and is cleaved by the target proteinase. In cleaved and latent serpins, the reactive site loop is inserted into a large central beta-sheet in the same molecule, whereas in ovalbumin, a nonfunctional serpin, the reactive site loop is completely exposed and in an alpha-helical conformation. However, in neither conformation can the reactive site loop bind to target proteinases. Here we report the structure of an intact and cleaved human antithrombin complex. The intact reactive site loop is in a novel conformation that seems well suited for interaction with proteinases such as thrombin and blood coagulation factor Xa.
 ==About this Structure==
-ATH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ATH OCA].
+ATH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ATH OCA].
 ==Reference==
@@ Line 14: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Hol, W.G.J.]]
+[[Category: Hol, W G.J.]]
-[[Category: Schreuder, H.A.]]
+[[Category: Schreuder, H A.]]
 [[Category: human antithrombin-iii]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:01:32 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:05 2008''