1rtg: Difference between revisions

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==Overview==

In common with most other matrix metalloproteinases, gelatinase A has a, non-catalytic C-terminal domain that displays sequence homology to, haemopexin. Crystals of this domain were used by molecular replacement to, solve its molecular structure at 2.6 A resolution, which was refined to an, R value of 17.9%. This structure has a disc-like shape, with the chain, folded into a beta-propeller structure that has pseudo four-fold symmetry., Although the topology and the side-chain arrangement are very similar to, the equivalent domain of fibroblast collagenase, significant differences, in surface charge and contouring are observable on 1 side of the, gelatinase A disc. This difference might be a factor in allowing the, gelatinase A C-terminal domain to bind to natural inhibitor TIMP-2.

In common with most other matrix metalloproteinases, gelatinase A has a non-catalytic C-terminal domain that displays sequence homology to haemopexin. Crystals of this domain were used by molecular replacement to solve its molecular structure at 2.6 A resolution, which was refined to an R value of 17.9%. This structure has a disc-like shape, with the chain folded into a beta-propeller structure that has pseudo four-fold symmetry. Although the topology and the side-chain arrangement are very similar to the equivalent domain of fibroblast collagenase, significant differences in surface charge and contouring are observable on 1 side of the gelatinase A disc. This difference might be a factor in allowing the gelatinase A C-terminal domain to bind to natural inhibitor TIMP-2.

==Disease==

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[[Category: metzincins]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 16~~:49:56 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:54:25 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-In common with most other matrix metalloproteinases, gelatinase A has a, non-catalytic C-terminal domain that displays sequence homology to, haemopexin. Crystals of this domain were used by molecular replacement to, solve its molecular structure at 2.6 A resolution, which was refined to an, R value of 17.9%. This structure has a disc-like shape, with the chain, folded into a beta-propeller structure that has pseudo four-fold symmetry., Although the topology and the side-chain arrangement are very similar to, the equivalent domain of fibroblast collagenase, significant differences, in surface charge and contouring are observable on 1 side of the, gelatinase A disc. This difference might be a factor in allowing the, gelatinase A C-terminal domain to bind to natural inhibitor TIMP-2.
+In common with most other matrix metalloproteinases, gelatinase A has a non-catalytic C-terminal domain that displays sequence homology to haemopexin. Crystals of this domain were used by molecular replacement to solve its molecular structure at 2.6 A resolution, which was refined to an R value of 17.9%. This structure has a disc-like shape, with the chain folded into a beta-propeller structure that has pseudo four-fold symmetry. Although the topology and the side-chain arrangement are very similar to the equivalent domain of fibroblast collagenase, significant differences in surface charge and contouring are observable on 1 side of the gelatinase A disc. This difference might be a factor in allowing the gelatinase A C-terminal domain to bind to natural inhibitor TIMP-2.
 ==Disease==
@@ Line 26: / Line 26: @@
 [[Category: metzincins]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:49:56 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:54:25 2008''