2oz4: Difference between revisions
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|PDB= 2oz4 |SIZE=350|CAPTION= <scene name='initialview01'>2oz4</scene>, resolution 2.70Å | |PDB= 2oz4 |SIZE=350|CAPTION= <scene name='initialview01'>2oz4</scene>, resolution 2.70Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ICAM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= ICAM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oz4 OCA], [http://www.ebi.ac.uk/pdbsum/2oz4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2oz4 RCSB]</span> | |||
}} | }} | ||
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[[Category: Song, G.]] | [[Category: Song, G.]] | ||
[[Category: Springer, T A.]] | [[Category: Springer, T A.]] | ||
[[Category: cell adhesion]] | [[Category: cell adhesion]] | ||
[[Category: cell-surface dimerization]] | [[Category: cell-surface dimerization]] | ||
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[[Category: structural plasticity]] | [[Category: structural plasticity]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:25:20 2008'' |
Revision as of 04:25, 31 March 2008
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, resolution 2.70Å | |||||||
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Ligands: | , , , , | ||||||
Gene: | ICAM1 (Homo sapiens) | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Structural Plasticity in IgSF Domain 4 of ICAM-1 Mediates Cell Surface Dimerization
OverviewOverview
The Ig superfamily (IgSF) intercellular adhesion molecule-1 (ICAM-1) equilibrates between monomeric and dimeric forms on the cell surface, and dimerization enhances cell adhesion. A crystal structure of ICAM-1 IgSF domains (D) 3-5 revealed a unique dimerization interface in which D4s of two protomers fuse through edge beta-strands to form a single super beta-sandwich domain. Here, we describe a crystal structure at 2.7-A resolution of monomeric ICAM-1 D3-D5, stabilized by the monomer-specific Fab CA7. CA7 binds to D5 in a region that is buried in the dimeric interface and is distal from the dimerization site in D4. In monomeric ICAM-1 D3-D5, a 16-residue loop in D4 that is disordered in the dimeric structure could clearly be traced as a BC loop, a short C strand, and a CE meander with a cis-Pro followed by a solvent-exposed, flexible four-residue region. Deletions of 6 or 10 residues showed that the C-strand is essential for monomer stability, whereas a distinct six-residue deletion showed little contribution of the CE meander. Mutation of two inward-pointing Leu residues in edge beta-strand E to Lys increased monomer stability, confirming the hypothesis that inward-pointing charged side chains on edge beta-strands are an important design feature to prevent beta-supersheet formation. Overall, the studies reveal that monomer-dimer transition is associated with a surprisingly large, physiologically relevant, IgSF domain rearrangement.
DiseaseDisease
Known disease associated with this structure: Malaria, cerebral, susceptibility to OMIM:[147840]
About this StructureAbout this Structure
2OZ4 is a Single protein structure of sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Structural plasticity in Ig superfamily domain 4 of ICAM-1 mediates cell surface dimerization., Chen X, Kim TD, Carman CV, Mi LZ, Song G, Springer TA, Proc Natl Acad Sci U S A. 2007 Sep 25;104(39):15358-63. Epub 2007 Sep 19. PMID:17881562
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