Category:SAP - Revision history

Bradley Monk at 23:04, 5 June 2013

2013-06-05T23:04:48Z

← Older revision		Revision as of 16:04, 5 June 2013
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			{{QualHeader}}

	==MAGUK==		==MAGUK==
	The membrane-associated guanylate kinases [[MAGUK]] are a superfamily of proteins.[1] The MAGUKs are defined by their inclusion of [[PDZ]], [[SH3]] and [[GUK]] domains, although many of them also contain regions homologous of [[CaMKII]], WW and L27 domains.[2] The GUK domain that they have is structurally very similar to that of the guanylate kinases, however it is known to be catalytically inactive as the P-Loop which binds ATP is absent. It is thought that the MAGUKs have subfunctionalized the GUK domain for their own purposes, primarily based on its ability to form protein-protein interactions with cytoskeleton proteins, microtubule/actin based machinery and molecules involved in signal transduction.		The membrane-associated guanylate kinases [[MAGUK]] are a superfamily of proteins.[1] The MAGUKs are defined by their inclusion of [[PDZ]], [[SH3]] and [[GUK]] domains, although many of them also contain regions homologous of [[CaMKII]], WW and L27 domains.[2] The GUK domain that they have is structurally very similar to that of the guanylate kinases, however it is known to be catalytically inactive as the P-Loop which binds ATP is absent. It is thought that the MAGUKs have subfunctionalized the GUK domain for their own purposes, primarily based on its ability to form protein-protein interactions with cytoskeleton proteins, microtubule/actin based machinery and molecules involved in signal transduction.

	The PDZ domain which are contained in the MAGUKs in varying numbers. PDZ domains are short peptide binding sequences commonly found at the C-terminus of interacting proteins. Copies within each of the family members often have different binding partners, due to amino acid differences between the copies. The SH3 domain is again a protein-protein interaction domain. Its family generally bind to PXXP sites, but in MAGUKs it is known to bind to other sites as well. One of the most well known features is that it can form an intramolecular bond with the GUK domain, creating what is known as a GUK-SH3 'closed' state.		The [[PDZ]] domain which are contained in the MAGUKs in varying numbers. [[PDZ]] domains are short peptide binding sequences commonly found at the C-terminus of interacting proteins. Copies within each of the family members often have different binding partners, due to amino acid differences between the copies. The SH3 domain is again a protein-protein interaction domain. Its family generally bind to PXXP sites, but in MAGUKs it is known to bind to other sites as well. One of the most well known features is that it can form an intramolecular bond with the GUK domain, creating what is known as a GUK-SH3 'closed' state.

	;Examples		;Examples

Bradley Monk at 22:35, 5 June 2013

2013-06-05T22:35:28Z

← Older revision		Revision as of 15:35, 5 June 2013
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	==MAGUK==		==MAGUK==
	The membrane-associated guanylate kinases (MAGUK) are a superfamily of proteins.[1] The MAGUKs are defined by their inclusion of PDZ, SH3 and GUK domains, although many of them also contain regions homologous of CaMKII, WW and L27 domains.[2] The GUK domain that they have is structurally very similar to that of the guanylate kinases, however it is known to be catalytically inactive as the P-Loop which binds ATP is absent. It is thought that the MAGUKs have subfunctionalized the GUK domain for their own purposes, primarily based on its ability to form protein-protein interactions with cytoskeleton proteins, microtubule/actin based machinery and molecules involved in signal transduction.		The membrane-associated guanylate kinases [[MAGUK]] are a superfamily of proteins.[1] The MAGUKs are defined by their inclusion of [[PDZ]], [[SH3]] and [[GUK]] domains, although many of them also contain regions homologous of [[CaMKII]], WW and L27 domains.[2] The GUK domain that they have is structurally very similar to that of the guanylate kinases, however it is known to be catalytically inactive as the P-Loop which binds ATP is absent. It is thought that the MAGUKs have subfunctionalized the GUK domain for their own purposes, primarily based on its ability to form protein-protein interactions with cytoskeleton proteins, microtubule/actin based machinery and molecules involved in signal transduction.

	The PDZ domain which are contained in the MAGUKs in varying numbers. PDZ domains are short peptide binding sequences commonly found at the C-terminus of interacting proteins. Copies within each of the family members often have different binding partners, due to amino acid differences between the copies. The SH3 domain is again a protein-protein interaction domain. Its family generally bind to PXXP sites, but in MAGUKs it is known to bind to other sites as well. One of the most well known features is that it can form an intramolecular bond with the GUK domain, creating what is known as a GUK-SH3 'closed' state.		The PDZ domain which are contained in the MAGUKs in varying numbers. PDZ domains are short peptide binding sequences commonly found at the C-terminus of interacting proteins. Copies within each of the family members often have different binding partners, due to amino acid differences between the copies. The SH3 domain is again a protein-protein interaction domain. Its family generally bind to PXXP sites, but in MAGUKs it is known to bind to other sites as well. One of the most well known features is that it can form an intramolecular bond with the GUK domain, creating what is known as a GUK-SH3 'closed' state.

	;Examples		;Examples
	*DLG1 = PSD97		*DLG1 (PSD97)
	*DLG2		*DLG2 (PSD93)
	*DLG3		*DLG3 (PSD102)
	*DLG4		*DLG4 ('''[[PSD95]]''', SAP90)
	*DLG5		*DLG5

Bradley Monk at 22:23, 5 June 2013

2013-06-05T22:23:06Z

← Older revision		Revision as of 15:23, 5 June 2013
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			==MAGUK==
	The membrane-associated guanylate kinases (MAGUK) are a superfamily of proteins.[1] The MAGUKs are defined by their inclusion of PDZ, SH3 and GUK domains, although many of them also contain regions homologous of CaMKII, WW and L27 domains.[2] The GUK domain that they have is structurally very similar to that of the guanylate kinases, however it is known to be catalytically inactive as the P-Loop which binds ATP is absent. It is thought that the MAGUKs have subfunctionalized the GUK domain for their own purposes, primarily based on its ability to form protein-protein interactions with cytoskeleton proteins, microtubule/actin based machinery and molecules involved in signal transduction.		The membrane-associated guanylate kinases (MAGUK) are a superfamily of proteins.[1] The MAGUKs are defined by their inclusion of PDZ, SH3 and GUK domains, although many of them also contain regions homologous of CaMKII, WW and L27 domains.[2] The GUK domain that they have is structurally very similar to that of the guanylate kinases, however it is known to be catalytically inactive as the P-Loop which binds ATP is absent. It is thought that the MAGUKs have subfunctionalized the GUK domain for their own purposes, primarily based on its ability to form protein-protein interactions with cytoskeleton proteins, microtubule/actin based machinery and molecules involved in signal transduction.
	The PDZ domain which are contained in the MAGUKs in varying numbers. PDZ domains are short peptide binding sequences commonly found at the C-terminus of interacting proteins. Copies within each of the family members often have different binding partners, due to amino acid differences between the copies. The SH3 domain is again a protein-protein interaction domain. Its family generally bind to PXXP sites, but in MAGUKs it is known to bind to other sites as well. One of the most well known features is that it can form an intramolecular bond with the GUK domain, creating what is known as a GUK-SH3 'closed' state.		The PDZ domain which are contained in the MAGUKs in varying numbers. PDZ domains are short peptide binding sequences commonly found at the C-terminus of interacting proteins. Copies within each of the family members often have different binding partners, due to amino acid differences between the copies. The SH3 domain is again a protein-protein interaction domain. Its family generally bind to PXXP sites, but in MAGUKs it is known to bind to other sites as well. One of the most well known features is that it can form an intramolecular bond with the GUK domain, creating what is known as a GUK-SH3 'closed' state.

			;Examples
			*DLG1 = PSD97
			*DLG2
			*DLG3
			*DLG4
			*DLG5

Bradley Monk: Created page with "The membrane-associated guanylate kinases (MAGUK) are a superfamily of proteins.[1] The MAGUKs are defined by their inclusion of PDZ, SH3 and GUK domains, although many of the..."

2013-06-05T22:19:59Z

Created page with "The membrane-associated guanylate kinases (MAGUK) are a superfamily of proteins.[1] The MAGUKs are defined by their inclusion of PDZ, SH3 and GUK domains, although many of the..."

New page

The membrane-associated guanylate kinases (MAGUK) are a superfamily of proteins.[1] The MAGUKs are defined by their inclusion of PDZ, SH3 and GUK domains, although many of them also contain regions homologous of CaMKII, WW and L27 domains.[2] The GUK domain that they have is structurally very similar to that of the guanylate kinases, however it is known to be catalytically inactive as the P-Loop which binds ATP is absent. It is thought that the MAGUKs have subfunctionalized the GUK domain for their own purposes, primarily based on its ability to form protein-protein interactions with cytoskeleton proteins, microtubule/actin based machinery and molecules involved in signal transduction.
The PDZ domain which are contained in the MAGUKs in varying numbers. PDZ domains are short peptide binding sequences commonly found at the C-terminus of interacting proteins. Copies within each of the family members often have different binding partners, due to amino acid differences between the copies. The SH3 domain is again a protein-protein interaction domain. Its family generally bind to PXXP sites, but in MAGUKs it is known to bind to other sites as well. One of the most well known features is that it can form an intramolecular bond with the GUK domain, creating what is known as a GUK-SH3 'closed' state.