1rsf: Difference between revisions

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

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

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

caption="1rsf" />

'''NMR Structure of Monomeric CAR d1 domain'''<br />

==Overview==

The coxsackievirus and adenovirus receptor (CAR) mediates entry of, coxsackievirus B (CVB) and adenovirus (Ad). The normal cellular function, of CAR, which is expressed in a wide variety of tissue types, is thought, to involve homophilic cell adhesion in the developing brain. The, extracellular domain of CAR consists of two immunoglobulin (Ig) domains, termed CAR-D1 and CAR-D2. CAR-D1 is shown by sedimentation velocity to be, monomeric at pH 3.0. The solution structure and the dynamic properties of, monomeric CAR-D1 have been determined by NMR spectroscopy at pH 3.0. The, determinants of the CAR-D1 monomer-dimer equilibrium, as well as the, binding site of CVB and Ad on CAR, are discussed in light of the monomer, structure.

The coxsackievirus and adenovirus receptor (CAR) mediates entry of coxsackievirus B (CVB) and adenovirus (Ad). The normal cellular function of CAR, which is expressed in a wide variety of tissue types, is thought to involve homophilic cell adhesion in the developing brain. The extracellular domain of CAR consists of two immunoglobulin (Ig) domains termed CAR-D1 and CAR-D2. CAR-D1 is shown by sedimentation velocity to be monomeric at pH 3.0. The solution structure and the dynamic properties of monomeric CAR-D1 have been determined by NMR spectroscopy at pH 3.0. The determinants of the CAR-D1 monomer-dimer equilibrium, as well as the binding site of CVB and Ad on CAR, are discussed in light of the monomer structure.

==Disease==

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==About this Structure==

1RSF 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=1RSF OCA].

1RSF 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=1RSF OCA].

==Reference==

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[[Category: Jacobs, A.]]

[[Category: Jiang, S.]]

[[Category: Laue, T.M.]]

[[Category: Laue, T M.]]

[[Category: adenovirus]]

[[Category: car]]

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[[Category: nmr]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 19~~:06:~~51 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:54:01 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1rsf.gif|left|200px]]<br />
+[[Image:1rsf.gif|left|200px]]<br /><applet load="1rsf" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1rsf" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1rsf" />
 '''NMR Structure of Monomeric CAR d1 domain'''<br />
 ==Overview==
-The coxsackievirus and adenovirus receptor (CAR) mediates entry of, coxsackievirus B (CVB) and adenovirus (Ad). The normal cellular function, of CAR, which is expressed in a wide variety of tissue types, is thought, to involve homophilic cell adhesion in the developing brain. The, extracellular domain of CAR consists of two immunoglobulin (Ig) domains, termed CAR-D1 and CAR-D2. CAR-D1 is shown by sedimentation velocity to be, monomeric at pH 3.0. The solution structure and the dynamic properties of, monomeric CAR-D1 have been determined by NMR spectroscopy at pH 3.0. The, determinants of the CAR-D1 monomer-dimer equilibrium, as well as the, binding site of CVB and Ad on CAR, are discussed in light of the monomer, structure.
+The coxsackievirus and adenovirus receptor (CAR) mediates entry of coxsackievirus B (CVB) and adenovirus (Ad). The normal cellular function of CAR, which is expressed in a wide variety of tissue types, is thought to involve homophilic cell adhesion in the developing brain. The extracellular domain of CAR consists of two immunoglobulin (Ig) domains termed CAR-D1 and CAR-D2. CAR-D1 is shown by sedimentation velocity to be monomeric at pH 3.0. The solution structure and the dynamic properties of monomeric CAR-D1 have been determined by NMR spectroscopy at pH 3.0. The determinants of the CAR-D1 monomer-dimer equilibrium, as well as the binding site of CVB and Ad on CAR, are discussed in light of the monomer structure.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-RSF 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=1RSF OCA].
+RSF 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=1RSF OCA].
 ==Reference==
@@ Line 20: / Line 19: @@
 [[Category: Jacobs, A.]]
 [[Category: Jiang, S.]]
-[[Category: Laue, T.M.]]
+[[Category: Laue, T M.]]
 [[Category: adenovirus]]
 [[Category: car]]
@@ Line 26: / Line 25: @@
 [[Category: nmr]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:06:51 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:54:01 2008''