1m1x
From Proteopedia
| Line 8: | Line 8: | ||
|GENE= | |GENE= | ||
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=smart00191 Int_alpha], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam08441 Integrin_alpha2], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam07965 Integrin_B_tail], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam00362 Integrin_beta]</span> | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=smart00191 Int_alpha], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam08441 Integrin_alpha2], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam07965 Integrin_B_tail], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam00362 Integrin_beta]</span> | ||
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1x OCA], [http://www.ebi.ac.uk/pdbsum/1m1x PDBsum | + | |RELATEDENTRY=[[1jv2|1JV2]], [[1m1u|1M1U]] |
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1x OCA], [http://www.ebi.ac.uk/pdbsum/1m1x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m1x RCSB]</span> | ||
}} | }} | ||
| Line 16: | Line 17: | ||
==Overview== | ==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. | 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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=173470 173470]] | ||
==About this Structure== | ==About this Structure== | ||
| Line 47: | Line 45: | ||
[[Category: thigh domain]] | [[Category: thigh domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:10:17 2008'' |
Revision as of 19:10, 30 March 2008
| |||||||
| , resolution 3.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Domains: | Int_alpha, Integrin_alpha2, Integrin_B_tail, Integrin_beta | ||||||
| Related: | 1JV2, 1M1U
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHA VBETA3 BOUND TO MN2+
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.
About this Structure
1M1X is a Protein complex structure of sequences from Homo sapiens. 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 Sun Mar 30 22:10:17 2008
Categories: Homo sapiens | Protein complex | Arnaout, M A. | Frech, M. | Goodman, S L. | Joachimiak, A. | Stehle, T. | Xiong, J P. | Zhang, R. | A-domain | Admida | Beta-tail domain | Cage motif | Calf domain | Egf domain | Genu | Hybrid domain | Mida | Propeller | Psi domain | Thigh domain
