2aav: Difference between revisions

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[[Image:2aav.gif|left|200px]]<br />

[[Image:2aav.gif|left|200px]]<br /><applet load="2aav" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="2aav" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2aav" />

'''Solution NMR structure of Filamin A domain 17'''<br />

==Overview==

Filamin A (FLNa), a dimeric actin cross-linking and scaffold protein with, numerous intracellular binding partners, anchors the platelet adhesion, glycoprotein (GP) Ib-IX-V receptor to actin cytoskeleton. We mapped the, GPIbalpha binding site to a single domain of FLNa and resolved the, structure of this domain and its interaction complex with the, corresponding GPIbalpha cytoplasmic domain. This is the first atomic, structure of this class of membrane glycoprotein-cytoskeleton connection., GPIbalpha binds in a groove formed between the C and D beta strands of, FLNa domain 17. The interaction is strikingly similar to that between the, beta7 integrin tail and a different FLNa domain, potentially defining a, conserved motif for FLNa binding. Nevertheless, the structures also reveal, specificity of the interfaces, which explains different regulatory, mechanisms. To verify the topology of GPIb-FLNa interaction we also, purified the native complex from platelets and showed that GPIb interacts, with the C-terminus of FLNa, which is in accordance with our biochemical, and structural data.

Filamin A (FLNa), a dimeric actin cross-linking and scaffold protein with numerous intracellular binding partners, anchors the platelet adhesion glycoprotein (GP) Ib-IX-V receptor to actin cytoskeleton. We mapped the GPIbalpha binding site to a single domain of FLNa and resolved the structure of this domain and its interaction complex with the corresponding GPIbalpha cytoplasmic domain. This is the first atomic structure of this class of membrane glycoprotein-cytoskeleton connection. GPIbalpha binds in a groove formed between the C and D beta strands of FLNa domain 17. The interaction is strikingly similar to that between the beta7 integrin tail and a different FLNa domain, potentially defining a conserved motif for FLNa binding. Nevertheless, the structures also reveal specificity of the interfaces, which explains different regulatory mechanisms. To verify the topology of GPIb-FLNa interaction we also purified the native complex from platelets and showed that GPIb interacts with the C-terminus of FLNa, which is in accordance with our biochemical and structural data.

==Disease==

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==About this Structure==

2AAV 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=2AAV OCA].

2AAV 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=2AAV OCA].

==Reference==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Hartwig, J.H.]]

[[Category: Hartwig, J H.]]

[[Category: Heikkinen, O.]]

[[Category: Kilpelainen, I.]]

[[Category: Munday, A.D.]]

[[Category: Munday, A D.]]

[[Category: Nakamura, F.]]

[[Category: Permi, P.]]

[[Category: Pudas, R.]]

[[Category: Stossel, T.P.]]

[[Category: Stossel, T P.]]

[[Category: Ylanne, J.]]

[[Category: beta-sandwich]]

[[Category: filamin a domain 17]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 20~~:48:~~09 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:25:36 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2aav.gif|left|200px]]<br />
+[[Image:2aav.gif|left|200px]]<br /><applet load="2aav" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2aav" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2aav" />
 '''Solution NMR structure of Filamin A domain 17'''<br />
 ==Overview==
-Filamin A (FLNa), a dimeric actin cross-linking and scaffold protein with, numerous intracellular binding partners, anchors the platelet adhesion, glycoprotein (GP) Ib-IX-V receptor to actin cytoskeleton. We mapped the, GPIbalpha binding site to a single domain of FLNa and resolved the, structure of this domain and its interaction complex with the, corresponding GPIbalpha cytoplasmic domain. This is the first atomic, structure of this class of membrane glycoprotein-cytoskeleton connection., GPIbalpha binds in a groove formed between the C and D beta strands of, FLNa domain 17. The interaction is strikingly similar to that between the, beta7 integrin tail and a different FLNa domain, potentially defining a, conserved motif for FLNa binding. Nevertheless, the structures also reveal, specificity of the interfaces, which explains different regulatory, mechanisms. To verify the topology of GPIb-FLNa interaction we also, purified the native complex from platelets and showed that GPIb interacts, with the C-terminus of FLNa, which is in accordance with our biochemical, and structural data.
+Filamin A (FLNa), a dimeric actin cross-linking and scaffold protein with numerous intracellular binding partners, anchors the platelet adhesion glycoprotein (GP) Ib-IX-V receptor to actin cytoskeleton. We mapped the GPIbalpha binding site to a single domain of FLNa and resolved the structure of this domain and its interaction complex with the corresponding GPIbalpha cytoplasmic domain. This is the first atomic structure of this class of membrane glycoprotein-cytoskeleton connection. GPIbalpha binds in a groove formed between the C and D beta strands of FLNa domain 17. The interaction is strikingly similar to that between the beta7 integrin tail and a different FLNa domain, potentially defining a conserved motif for FLNa binding. Nevertheless, the structures also reveal specificity of the interfaces, which explains different regulatory mechanisms. To verify the topology of GPIb-FLNa interaction we also purified the native complex from platelets and showed that GPIb interacts with the C-terminus of FLNa, which is in accordance with our biochemical and structural data.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-AAV 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=2AAV OCA].
+AAV 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=2AAV OCA].
 ==Reference==
@@ Line 17: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Hartwig, J.H.]]
+[[Category: Hartwig, J H.]]
 [[Category: Heikkinen, O.]]
 [[Category: Kilpelainen, I.]]
-[[Category: Munday, A.D.]]
+[[Category: Munday, A D.]]
 [[Category: Nakamura, F.]]
 [[Category: Permi, P.]]
 [[Category: Pudas, R.]]
-[[Category: Stossel, T.P.]]
+[[Category: Stossel, T P.]]
 [[Category: Ylanne, J.]]
 [[Category: beta-sandwich]]
 [[Category: filamin a domain 17]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:48:09 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:25:36 2008''