2oz4: Difference between revisions
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{{STRUCTURE_2oz4| PDB=2oz4 | SCENE= }} | |||
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'''Structural Plasticity in IgSF Domain 4 of ICAM-1 Mediates Cell Surface Dimerization''' | '''Structural Plasticity in IgSF Domain 4 of ICAM-1 Mediates Cell Surface Dimerization''' | ||
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[[Category: Song, G.]] | [[Category: Song, G.]] | ||
[[Category: Springer, T A.]] | [[Category: Springer, T A.]] | ||
[[Category: | [[Category: Cell adhesion]] | ||
[[Category: | [[Category: Cell-surface dimerization]] | ||
[[Category: | [[Category: Igsf domain]] | ||
[[Category: | [[Category: Structural plasticity]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:58:15 2008'' | |||
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Revision as of 11:58, 4 May 2008
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 Page seeded by OCA on Sun May 4 11:58:15 2008