2i9b: Difference between revisions

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==Overview==

Recent studies indicate that binding of the urokinase-type plasminogen, activator (uPA) to its high-affinity receptor (uPAR) orchestrates uPAR, interactions with other cellular components that play a pivotal role in, diverse (patho-)physiological processes, including wound healing, angiogenesis, inflammation, and cancer metastasis. However, notwithstanding the wealth of biochemical data available describing the, activities of uPAR, little is known about the exact mode of uPAR/uPA, interactions or the presumed conformational changes that accompany, uPA/uPAR engagement. Here, we report the crystal structure of soluble, urokinase plasminogen activator receptor (suPAR), which contains the three, domains of the wild-type receptor but lacks the cell-surface anchoring, sequence, in complex with the amino-terminal fragment of urokinase-type, plasminogen activator (ATF), at the resolution of 2.8 A. We report the 1.9, A crystal structure of free ATF. Our results provide a structural basis, represented by conformational changes induced in uPAR, for several, published biochemical observations describing the nature of uPAR/uPA, interactions and provide insight into mechanisms that may be responsible, for the cellular responses induced by uPA binding.

Recent studies indicate that binding of the urokinase-type plasminogen activator (uPA) to its high-affinity receptor (uPAR) orchestrates uPAR interactions with other cellular components that play a pivotal role in diverse (patho-)physiological processes, including wound healing, angiogenesis, inflammation, and cancer metastasis. However, notwithstanding the wealth of biochemical data available describing the activities of uPAR, little is known about the exact mode of uPAR/uPA interactions or the presumed conformational changes that accompany uPA/uPAR engagement. Here, we report the crystal structure of soluble urokinase plasminogen activator receptor (suPAR), which contains the three domains of the wild-type receptor but lacks the cell-surface anchoring sequence, in complex with the amino-terminal fragment of urokinase-type plasminogen activator (ATF), at the resolution of 2.8 A. We report the 1.9 A crystal structure of free ATF. Our results provide a structural basis, represented by conformational changes induced in uPAR, for several published biochemical observations describing the nature of uPAR/uPA interactions and provide insight into mechanisms that may be responsible for the cellular responses induced by uPA binding.

==Disease==

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[[Category: urokinase receptor]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Recent studies indicate that binding of the urokinase-type plasminogen, activator (uPA) to its high-affinity receptor (uPAR) orchestrates uPAR, interactions with other cellular components that play a pivotal role in, diverse (patho-)physiological processes, including wound healing, angiogenesis, inflammation, and cancer metastasis. However, notwithstanding the wealth of biochemical data available describing the, activities of uPAR, little is known about the exact mode of uPAR/uPA, interactions or the presumed conformational changes that accompany, uPA/uPAR engagement. Here, we report the crystal structure of soluble, urokinase plasminogen activator receptor (suPAR), which contains the three, domains of the wild-type receptor but lacks the cell-surface anchoring, sequence, in complex with the amino-terminal fragment of urokinase-type, plasminogen activator (ATF), at the resolution of 2.8 A. We report the 1.9, A crystal structure of free ATF. Our results provide a structural basis, represented by conformational changes induced in uPAR, for several, published biochemical observations describing the nature of uPAR/uPA, interactions and provide insight into mechanisms that may be responsible, for the cellular responses induced by uPA binding.
+Recent studies indicate that binding of the urokinase-type plasminogen activator (uPA) to its high-affinity receptor (uPAR) orchestrates uPAR interactions with other cellular components that play a pivotal role in diverse (patho-)physiological processes, including wound healing, angiogenesis, inflammation, and cancer metastasis. However, notwithstanding the wealth of biochemical data available describing the activities of uPAR, little is known about the exact mode of uPAR/uPA interactions or the presumed conformational changes that accompany uPA/uPAR engagement. Here, we report the crystal structure of soluble urokinase plasminogen activator receptor (suPAR), which contains the three domains of the wild-type receptor but lacks the cell-surface anchoring sequence, in complex with the amino-terminal fragment of urokinase-type plasminogen activator (ATF), at the resolution of 2.8 A. We report the 1.9 A crystal structure of free ATF. Our results provide a structural basis, represented by conformational changes induced in uPAR, for several published biochemical observations describing the nature of uPAR/uPA interactions and provide insight into mechanisms that may be responsible for the cellular responses induced by uPA binding.
 ==Disease==
@@ Line 24: / Line 24: @@
 [[Category: urokinase receptor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:35:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:50:16 2008''