1l5g
From Proteopedia
(New page: 200px<br /> <applet load="1l5g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l5g, resolution 3.2Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1l5g.gif|left|200px]]<br /> | + | [[Image:1l5g.gif|left|200px]]<br /><applet load="1l5g" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1l5g" size=" | + | |
caption="1l5g, resolution 3.2Å" /> | caption="1l5g, resolution 3.2Å" /> | ||
'''CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN AVB3 IN COMPLEX WITH AN ARG-GLY-ASP LIGAND'''<br /> | '''CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN AVB3 IN COMPLEX WITH AN ARG-GLY-ASP LIGAND'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structural basis for the divalent cation-dependent binding of | + | The structural basis for the divalent cation-dependent binding of heterodimeric alphabeta integrins to their ligands, which contain the prototypical Arg-Gly-Asp sequence, is unknown. Interaction with ligands triggers tertiary and quaternary structural rearrangements in integrins that are needed for cell signaling. Here we report the crystal structure of the extracellular segment of integrin alphaVbeta3 in complex with a cyclic peptide presenting the Arg-Gly-Asp sequence. The ligand binds at the major interface between the alphaV and beta3 subunits and makes extensive contacts with both. Both tertiary and quaternary changes are observed in the presence of ligand. The tertiary rearrangements take place in betaA, the ligand-binding domain of beta3; in the complex, betaA acquires two cations, one of which contacts the ligand Asp directly and the other stabilizes the ligand-binding surface. Ligand binding induces small changes in the orientation of alphaV relative to beta3. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1L5G 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 MN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1L5G 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=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L5G OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Arnaout, M | + | [[Category: Arnaout, M A.]] |
[[Category: Frech, M.]] | [[Category: Frech, M.]] | ||
| - | [[Category: Goodman, S | + | [[Category: Goodman, S L.]] |
[[Category: Joachimiak, A.]] | [[Category: Joachimiak, A.]] | ||
[[Category: Stehle, T.]] | [[Category: Stehle, T.]] | ||
| - | [[Category: Xiong, J | + | [[Category: Xiong, J P.]] |
[[Category: Zhang, R.]] | [[Category: Zhang, R.]] | ||
[[Category: MN]] | [[Category: MN]] | ||
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[[Category: thigh domain]] | [[Category: thigh domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:41:37 2008'' |
Revision as of 11:41, 21 February 2008
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CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN AVB3 IN COMPLEX WITH AN ARG-GLY-ASP LIGAND
Contents |
Overview
The structural basis for the divalent cation-dependent binding of heterodimeric alphabeta integrins to their ligands, which contain the prototypical Arg-Gly-Asp sequence, is unknown. Interaction with ligands triggers tertiary and quaternary structural rearrangements in integrins that are needed for cell signaling. Here we report the crystal structure of the extracellular segment of integrin alphaVbeta3 in complex with a cyclic peptide presenting the Arg-Gly-Asp sequence. The ligand binds at the major interface between the alphaV and beta3 subunits and makes extensive contacts with both. Both tertiary and quaternary changes are observed in the presence of ligand. The tertiary rearrangements take place in betaA, the ligand-binding domain of beta3; in the complex, betaA acquires two cations, one of which contacts the ligand Asp directly and the other stabilizes the ligand-binding surface. Ligand binding induces small changes in the orientation of alphaV relative to beta3.
Disease
Known diseases associated with this structure: Glanzmann thrombasthenia, type B OMIM:[173470]
About this Structure
1L5G 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 in complex with an Arg-Gly-Asp ligand., Xiong JP, Stehle T, Zhang R, Joachimiak A, Frech M, Goodman SL, Arnaout MA, Science. 2002 Apr 5;296(5565):151-5. Epub 2002 Mar 7. PMID:11884718
Page seeded by OCA on Thu Feb 21 13:41:37 2008
Categories: Homo sapiens | Protein complex | Arnaout, M A. | Frech, M. | Goodman, S L. | Joachimiak, A. | Stehle, T. | Xiong, J P. | Zhang, R. | MN | NAG | A-domain | Admidas | Beta-tail domain | Cage motif | Calf domain | Egf domain | Genu | Hybrid domain | Limbs | Midas | Propeller | Psi domain | Rgd ligand | Thigh domain
