1jv2

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(New page: 200px<br /> <applet load="1jv2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jv2, resolution 3.1&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1jv2.gif|left|200px]]<br /><applet load="1jv2" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1jv2" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1jv2, resolution 3.1&Aring;" />
caption="1jv2, resolution 3.1&Aring;" />
'''CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHAVBETA3'''<br />
'''CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHAVBETA3'''<br />
==Overview==
==Overview==
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Integrins are alphabeta heterodimeric receptors that mediate divalent, cation-dependent cell-cell and cell-matrix adhesion through tightly, regulated interactions with ligands. We have solved the crystal structure, of the extracellular portion of integrin alphaVbeta3 at 3.1 A resolution., Its 12 domains assemble into an ovoid "head" and two "tails." In the, crystal, alphaVbeta3 is severely bent at a defined region in its tails, reflecting an unusual flexibility that may be linked to integrin, regulation. The main inter-subunit interface lies within the head, between, a seven-bladed beta-propeller from alphaV and an A domain from beta3, and, bears a striking resemblance to the Galpha/Gbeta interface in G proteins., A metal ion-dependent adhesion site (MIDAS) in the betaA domain is, positioned to participate in a ligand-binding interface formed of loops, from the propeller and betaA domains. MIDAS lies adjacent to a, calcium-binding site with a potential regulatory function.
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Integrins are alphabeta heterodimeric receptors that mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands. We have solved the crystal structure of the extracellular portion of integrin alphaVbeta3 at 3.1 A resolution. Its 12 domains assemble into an ovoid "head" and two "tails." In the crystal, alphaVbeta3 is severely bent at a defined region in its tails, reflecting an unusual flexibility that may be linked to integrin regulation. The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins. A metal ion-dependent adhesion site (MIDAS) in the betaA domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and betaA domains. MIDAS lies adjacent to a calcium-binding site with a potential regulatory function.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1JV2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JV2 OCA].
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1JV2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JV2 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Arnaout, M.A.]]
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[[Category: Arnaout, M A.]]
[[Category: Diefenbach, B.]]
[[Category: Diefenbach, B.]]
[[Category: Dunker, R.]]
[[Category: Dunker, R.]]
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[[Category: Goodman, S.L.]]
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[[Category: Goodman, S L.]]
[[Category: Joachimiak, A.]]
[[Category: Joachimiak, A.]]
[[Category: Scott, D.]]
[[Category: Scott, D.]]
[[Category: Stehle, T.]]
[[Category: Stehle, T.]]
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[[Category: Xiong, J.P.]]
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[[Category: Xiong, J P.]]
[[Category: Zhang, R.]]
[[Category: Zhang, R.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: thigh domain]]
[[Category: thigh domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:44:45 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:27:04 2008''

Revision as of 11:27, 21 February 2008


1jv2, resolution 3.1Å

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CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHAVBETA3

Contents

Overview

Integrins are alphabeta heterodimeric receptors that mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands. We have solved the crystal structure of the extracellular portion of integrin alphaVbeta3 at 3.1 A resolution. Its 12 domains assemble into an ovoid "head" and two "tails." In the crystal, alphaVbeta3 is severely bent at a defined region in its tails, reflecting an unusual flexibility that may be linked to integrin regulation. The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins. A metal ion-dependent adhesion site (MIDAS) in the betaA domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and betaA domains. MIDAS lies adjacent to a calcium-binding site with a potential regulatory function.

Disease

Known disease associated with this structure: Glanzmann thrombasthenia, type B OMIM:[173470]

About this Structure

1JV2 is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the extracellular segment of integrin alpha Vbeta3., Xiong JP, Stehle T, Diefenbach B, Zhang R, Dunker R, Scott DL, Joachimiak A, Goodman SL, Arnaout MA, Science. 2001 Oct 12;294(5541):339-45. Epub 2001 Sep 6. PMID:11546839

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