2vh8 - Revision history

OCA: Redirecting to 2wqz

OCA — Wed, 09 Sep 2009 06:15:18 GMT

Redirecting to 2wqz

←Older revision		Revision as of 06:15, 9 September 2009
Line 1:		Line 1:
-	~~{{Seed}}~~	+	#REDIRECT [[2wqz]] This PDB entry is obsolete and replaced by 2wqz
-	[[~~Image:2vh8.png\|left\|200px~~]]	+
-		+
-	~~<!--~~	+
-	~~The line below this paragraph, containing "STRUCTURE_2vh8", creates the "Structure Box" on the page.~~	+
-	~~You may change the~~ PDB ~~parameter (which sets the PDB file loaded into the applet)~~	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page~~ is ~~loaded),~~	+
-	~~or leave the SCENE parameter empty for the default display.~~	+
-	~~-->~~	+
-	~~{{STRUCTURE_2vh8\| PDB=2vh8 \| SCENE= }}~~	+
-		+
-	~~===CRYSTAL STRUCTURE OF SYNAPTIC PROTEIN NEUROLIGIN 4 IN COMPLEX WITH NEUREXIN BETA 1.===~~	+
-		+
-		+
-	~~<!--~~	+
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_18093521}}, adds the Publication Abstract to the page~~	+
-	~~(as it appears on PubMed at http://www.pubmed.gov), where 18093521 is the PubMed ID number.~~	+
-	~~-->~~	+
-	~~{{ABSTRACT_PUBMED_18093521}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~2VH8 is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]~~ and ~~[http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VH8 OCA].~~	+
-		+
-	~~==Reference==~~	+
-	~~<ref group="xtra">PMID:18093521</ref><references group="xtra"/>~~	+
-	~~[[Category: Homo sapiens]]~~	+
-	~~[[Category: Rattus norvegicus]]~~	+
-	~~[[Category: Bourne, Y.]]~~	+
-	~~[[Category: Comoletti, D.]]~~	+
-	~~[[Category: Fabrichny, I P.]]~~	+
-	~~[[Category: Leone, P.]]~~	+
-	~~[[Category: Marchot, P.]]~~	+
-	~~[[Category: Miller, M T.]]~~	+
-	~~[[Category: Sulzenbacher, G.]]~~	+
-	~~[[Category: Taylor, P.]]~~	+
-	~~[[Category: Alternative promoter usage]]~~	+
-	~~[[Category: Alternative splicing]]~~	+
-	~~[[Category: Cell adhesion]]~~	+
-	~~[[Category: Cell adhesion alpha/beta-hydrolase cholinesterase autism b]]~~	+
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Membrane]]~~	+
-	~~[[Category: Transmembrane]]~~	+
-		+
-	~~''Page seeded~~ by ~~[http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 14:38:36 2009''~~	+

OCA at 12:38, 17 February 2009

OCA — Tue, 17 Feb 2009 12:38:37 GMT

←Older revision		Revision as of 12:38, 17 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	2VH8 is a ~~[[Protein complex]]~~ structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VH8 OCA].	+	2VH8 is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VH8 OCA].

	==Reference==		==Reference==
-	Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion., Fabrichny IP, Leone P, Sulzenbacher G, Comoletti D, Miller MT, Taylor P, Bourne Y, Marchot P, Neuron. 2007 Dec 20;56(6):979-91. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/18093521 18093521]~~	+	<ref group="xtra">PMID:18093521</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Protein complex]]
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
	[[Category: Bourne, Y.]]		[[Category: Bourne, Y.]]
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	[[Category: Transmembrane]]		[[Category: Transmembrane]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Mon Jul 28 20~~:06:~~27 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 14:38:36 2009''

OCA at 17:06, 28 July 2008

OCA — Mon, 28 Jul 2008 17:06:29 GMT

←Older revision		Revision as of 17:06, 28 July 2008
Line 1:		Line 1:
-	[[Image:2vh8.~~jpg~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:2vh8.png\|left\|200px]]

	<!--		<!--
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	{{STRUCTURE_2vh8\| PDB=2vh8 \| SCENE= }}		{{STRUCTURE_2vh8\| PDB=2vh8 \| SCENE= }}

-	~~'''~~CRYSTAL STRUCTURE OF SYNAPTIC PROTEIN NEUROLIGIN 4 IN COMPLEX WITH NEUREXIN BETA 1.~~'''~~	+	===CRYSTAL STRUCTURE OF SYNAPTIC PROTEIN NEUROLIGIN 4 IN COMPLEX WITH NEUREXIN BETA 1.===


-	~~==Overview==~~	+	<!--
-	The ~~neuroligins are postsynaptic cell adhesion proteins whose associations with presynaptic neurexins participate in synaptogenesis. Mutations in~~ the ~~neuroligin and neurexin genes appear~~ to ~~be associated with autism and mental retardation~~. ~~The crystal structure of a neuroligin reveals features not found in its catalytically active relatives~~, ~~such as~~ the fully hydrophobic interface forming the functional neuroligin dimer; the conformations of surface loops surrounding the vestigial active center; the location of determinants that are critical for folding and processing; and the absence of a macromolecular dipole and presence of an electronegative, hydrophilic surface for neurexin binding. ~~The structure of a beta~~-~~neurexin~~-neuroligin complex reveals the precise orientation of the bound neurexin and, despite a limited resolution, provides substantial information on the Ca2+-dependent interactions network involved in trans-synaptic neurexin-neuroligin association. These structures exemplify how an alpha/beta-hydrolase fold varies in surface topography to confer adhesion properties and provide templates for analyzing abnormal processing or recognition events associated with autism.	+	The line below this paragraph, {{ABSTRACT_PUBMED_18093521}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 18093521 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_18093521}}

	==About this Structure==		==About this Structure==
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	[[Category: Membrane]]		[[Category: Membrane]]
	[[Category: Transmembrane]]		[[Category: Transmembrane]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 18~~:48:28 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:06:27 2008''

OCA at 15:48, 4 May 2008

OCA — Sun, 04 May 2008 15:48:28 GMT

←Older revision		Revision as of 15:48, 4 May 2008
Line 1:		Line 1:
	[[Image:2vh8.jpg\|left\|200px]]		[[Image:2vh8.jpg\|left\|200px]]

-	{{Structure	+	<!--
-	\|PDB~~= 2vh8 \|SIZE=350\|CAPTION= <~~scene ~~name='initialview01'>2vh8</scene>~~, ~~resolution 3~~.~~90Å~~	+	The line below this paragraph, containing "STRUCTURE_2vh8", creates the "Structure Box" on the page.
-	~~\|SITE=~~	+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	~~\|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene~~>	+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	\|~~ACTIVITY~~=	+	or leave the SCENE parameter empty for the default display.
-	\|~~GENE~~=	+	-->
-	~~\|DOMAIN=~~	+	{{STRUCTURE_2vh8\| PDB=2vh8 \| SCENE= }}
-	~~\|RELATEDENTRY=[[1c4r\|1C4R]]~~	+
-	\|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vh8 OCA], [http://www.ebi.ac.uk/pdbsum/2vh8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vh8 RCSB]</span>	+
-	}}	+

	'''CRYSTAL STRUCTURE OF SYNAPTIC PROTEIN NEUROLIGIN 4 IN COMPLEX WITH NEUREXIN BETA 1.'''		'''CRYSTAL STRUCTURE OF SYNAPTIC PROTEIN NEUROLIGIN 4 IN COMPLEX WITH NEUREXIN BETA 1.'''
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	[[Category: Sulzenbacher, G.]]		[[Category: Sulzenbacher, G.]]
	[[Category: Taylor, P.]]		[[Category: Taylor, P.]]
-	[[Category: ~~alternative~~ promoter usage]]	+	[[Category: Alternative promoter usage]]
-	[[Category: ~~alternative~~ splicing]]	+	[[Category: Alternative splicing]]
-	[[Category: ~~cell~~ adhesion]]	+	[[Category: Cell adhesion]]
-	[[Category: ~~cell~~ adhesion alpha/beta-hydrolase cholinesterase autism b]]	+	[[Category: Cell adhesion alpha/beta-hydrolase cholinesterase autism b]]
-	[[Category: ~~glycoprotein~~]]	+	[[Category: Glycoprotein]]
-	[[Category: ~~membrane~~]]	+	[[Category: Membrane]]
-	[[Category: ~~transmembrane~~]]	+	[[Category: Transmembrane]]
-		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:48:28 2008''
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Mon Mar 31 05~~:12:16 2008''	+

OCA at 02:12, 31 March 2008

OCA — Mon, 31 Mar 2008 02:12:16 GMT

←Older revision		Revision as of 02:12, 31 March 2008
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	\|PDB= 2vh8 \|SIZE=350\|CAPTION= <scene name='initialview01'>2vh8</scene>, resolution 3.90Å		\|PDB= 2vh8 \|SIZE=350\|CAPTION= <scene name='initialview01'>2vh8</scene>, resolution 3.90Å
	\|SITE=		\|SITE=
-	\|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>	+	\|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
	\|ACTIVITY=		\|ACTIVITY=
	\|GENE=		\|GENE=
		+	\|DOMAIN=
		+	\|RELATEDENTRY=[[1c4r\|1C4R]]
		+	\|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vh8 OCA], [http://www.ebi.ac.uk/pdbsum/2vh8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vh8 RCSB]</span>
	}}		}}

Line 31:		Line 34:
	[[Category: Sulzenbacher, G.]]		[[Category: Sulzenbacher, G.]]
	[[Category: Taylor, P.]]		[[Category: Taylor, P.]]
-	[[Category: CA]]
	[[Category: alternative promoter usage]]		[[Category: alternative promoter usage]]
	[[Category: alternative splicing]]		[[Category: alternative splicing]]
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	[[Category: transmembrane]]		[[Category: transmembrane]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu~~ Mar ~~20 18~~:46:42 2008''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:12:16 2008''

OCA at 16:46, 20 March 2008

OCA — Thu, 20 Mar 2008 16:46:43 GMT

←Older revision		Revision as of 16:46, 20 March 2008
Line 1:		Line 1:
-	[[Image:2vh8.jpg\|left\|200px]]~~<br /><applet load~~="2vh8~~" size~~="350~~" color~~=~~"white" frame~~=~~"true" align="right" spinBox="true"~~	+	[[Image:2vh8.jpg\|left\|200px]]
-	~~caption="~~2vh8, resolution 3.90Å" />	+
-	'''CRYSTAL STRUCTURE OF SYNAPTIC PROTEIN NEUROLIGIN 4 IN COMPLEX WITH NEUREXIN BETA 1.'''~~<br />~~	+	{{Structure
		+	\|PDB= 2vh8 \|SIZE=350\|CAPTION= <scene name='initialview01'>2vh8</scene>, resolution 3.90Å
		+	\|SITE=
		+	\|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
		+	\|ACTIVITY=
		+	\|GENE=
		+	}}
		+
		+	'''CRYSTAL STRUCTURE OF SYNAPTIC PROTEIN NEUROLIGIN 4 IN COMPLEX WITH NEUREXIN BETA 1.'''
		+

	==Overview==		==Overview==
Line 7:		Line 16:

	==About this Structure==		==About this Structure==
-	2VH8 is a [~~http://en.wikipedia.org/wiki/Protein_complex~~ Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus~~] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VH8 OCA].	+	2VH8 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VH8 OCA].

	==Reference==		==Reference==
-	Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion., Fabrichny IP, Leone P, Sulzenbacher G, Comoletti D, Miller MT, Taylor P, Bourne Y, Marchot P, Neuron. 2007 Dec 20;56(6):979-91. PMID:[http://~~ispc~~.~~weizmann~~.ac.~~il/~~/~~pmbin~~/~~getpm?pmid=~~18093521 18093521]	+	Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion., Fabrichny IP, Leone P, Sulzenbacher G, Comoletti D, Miller MT, Taylor P, Bourne Y, Marchot P, Neuron. 2007 Dec 20;56(6):979-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18093521 18093521]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Protein complex]]		[[Category: Protein complex]]
Line 31:		Line 40:
	[[Category: transmembrane]]		[[Category: transmembrane]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu ~~Feb 21~~ 18:55:56 2008''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:46:42 2008''

OCA at 16:55, 21 February 2008

OCA — Thu, 21 Feb 2008 16:55:57 GMT

←Older revision		Revision as of 16:55, 21 February 2008
Line 4:		Line 4:

	==Overview==		==Overview==
-	The neuroligins are postsynaptic cell adhesion proteins whose associations, with presynaptic neurexins participate in synaptogenesis. Mutations in the, neuroligin and neurexin genes appear to be associated with autism and, mental retardation. The crystal structure of a neuroligin reveals features, not found in its catalytically active relatives, such as the fully, hydrophobic interface forming the functional neuroligin dimer; the, conformations of surface loops surrounding the vestigial active center;, the location of determinants that are critical for folding and processing;, and the absence of a macromolecular dipole and presence of an, electronegative, hydrophilic surface for neurexin binding. The structure, of a beta-neurexin-neuroligin complex reveals the precise orientation of, the bound neurexin and, despite a limited resolution, provides substantial, information on the ~~Ca(2~~+)-dependent interactions network involved in, trans-synaptic neurexin-neuroligin association. These structures exemplify, how an alpha/beta-hydrolase fold varies in surface topography to confer, adhesion properties and provide templates for analyzing abnormal, processing or recognition events associated with autism.	+	The neuroligins are postsynaptic cell adhesion proteins whose associations with presynaptic neurexins participate in synaptogenesis. Mutations in the neuroligin and neurexin genes appear to be associated with autism and mental retardation. The crystal structure of a neuroligin reveals features not found in its catalytically active relatives, such as the fully hydrophobic interface forming the functional neuroligin dimer; the conformations of surface loops surrounding the vestigial active center; the location of determinants that are critical for folding and processing; and the absence of a macromolecular dipole and presence of an electronegative, hydrophilic surface for neurexin binding. The structure of a beta-neurexin-neuroligin complex reveals the precise orientation of the bound neurexin and, despite a limited resolution, provides substantial information on the Ca2+-dependent interactions network involved in trans-synaptic neurexin-neuroligin association. These structures exemplify how an alpha/beta-hydrolase fold varies in surface topography to confer adhesion properties and provide templates for analyzing abnormal processing or recognition events associated with autism.

	==About this Structure==		==About this Structure==
Line 10:		Line 10:

	==Reference==		==Reference==
-	Structural ~~Analysis~~ of the ~~Synaptic Protein Neuroligin~~ and ~~Its~~ beta-~~Neurexin Complex~~: ~~Determinants~~ for ~~Folding~~ and ~~Cell Adhesion~~., Fabrichny IP, Leone P, Sulzenbacher G, Comoletti D, Miller MT, Taylor P, Bourne Y, Marchot P, Neuron. 2007 Dec 20;56(6):979-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18093521 18093521]	+	Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion., Fabrichny IP, Leone P, Sulzenbacher G, Comoletti D, Miller MT, Taylor P, Bourne Y, Marchot P, Neuron. 2007 Dec 20;56(6):979-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18093521 18093521]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Protein complex]]		[[Category: Protein complex]]
Line 16:		Line 16:
	[[Category: Bourne, Y.]]		[[Category: Bourne, Y.]]
	[[Category: Comoletti, D.]]		[[Category: Comoletti, D.]]
-	[[Category: Fabrichny, I.P.]]	+	[[Category: Fabrichny, I P.]]
	[[Category: Leone, P.]]		[[Category: Leone, P.]]
	[[Category: Marchot, P.]]		[[Category: Marchot, P.]]
-	[[Category: Miller, M.T.]]	+	[[Category: Miller, M T.]]
	[[Category: Sulzenbacher, G.]]		[[Category: Sulzenbacher, G.]]
	[[Category: Taylor, P.]]		[[Category: Taylor, P.]]
Line 31:		Line 31:
	[[Category: transmembrane]]		[[Category: transmembrane]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Jan 23 11~~:04:28 2008''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:55:56 2008''

OCA: New page: 200px
'''CRYSTAL STRUCTURE OF...
OCA — Wed, 23 Jan 2008 09:04:29 GMT

New page: 200px<br /><applet load="2vh8" size="350" color="white" frame="true" align="right" spinBox="true" caption="2vh8, resolution 3.90Å" /> '''CRYSTAL STRUCTURE OF...

New page
[[Image:2vh8.jpg|left|200px]]<br /><applet load="2vh8" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2vh8, resolution 3.90Å" />
'''CRYSTAL STRUCTURE OF SYNAPTIC PROTEIN NEUROLIGIN 4 IN COMPLEX WITH NEUREXIN BETA 1.'''<br />

==Overview==
The neuroligins are postsynaptic cell adhesion proteins whose associations, with presynaptic neurexins participate in synaptogenesis. Mutations in the, neuroligin and neurexin genes appear to be associated with autism and, mental retardation. The crystal structure of a neuroligin reveals features, not found in its catalytically active relatives, such as the fully, hydrophobic interface forming the functional neuroligin dimer; the, conformations of surface loops surrounding the vestigial active center;, the location of determinants that are critical for folding and processing;, and the absence of a macromolecular dipole and presence of an, electronegative, hydrophilic surface for neurexin binding. The structure, of a beta-neurexin-neuroligin complex reveals the precise orientation of, the bound neurexin and, despite a limited resolution, provides substantial, information on the Ca(2+)-dependent interactions network involved in, trans-synaptic neurexin-neuroligin association. These structures exemplify, how an alpha/beta-hydrolase fold varies in surface topography to confer, adhesion properties and provide templates for analyzing abnormal, processing or recognition events associated with autism.

==About this Structure==
2VH8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VH8 OCA].

==Reference==
Structural Analysis of the Synaptic Protein Neuroligin and Its beta-Neurexin Complex: Determinants for Folding and Cell Adhesion., Fabrichny IP, Leone P, Sulzenbacher G, Comoletti D, Miller MT, Taylor P, Bourne Y, Marchot P, Neuron. 2007 Dec 20;56(6):979-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18093521 18093521]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Bourne, Y.]]
[[Category: Comoletti, D.]]
[[Category: Fabrichny, I.P.]]
[[Category: Leone, P.]]
[[Category: Marchot, P.]]
[[Category: Miller, M.T.]]
[[Category: Sulzenbacher, G.]]
[[Category: Taylor, P.]]
[[Category: CA]]
[[Category: alternative promoter usage]]
[[Category: alternative splicing]]
[[Category: cell adhesion]]
[[Category: cell adhesion alpha/beta-hydrolase cholinesterase autism b]]
[[Category: glycoprotein]]
[[Category: membrane]]
[[Category: transmembrane]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:04:28 2008''