View source for 2oz4

[[Image:2oz4.gif|left|200px]]

 {{Structure
|PDB= 2oz4 |SIZE=350|CAPTION= <scene name='initialview01'>2oz4</scene>, resolution 2.70&Aring;
|SITE= 
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
|ACTIVITY= 
|GENE= ICAM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
}}

'''Structural Plasticity in IgSF Domain 4 of ICAM-1 Mediates Cell Surface Dimerization'''


==Overview==
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.

==Disease==
Known disease associated with this structure: Malaria, cerebral, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147840 147840]]

==About this Structure==
2OZ4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OZ4 OCA]. 

==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/17881562 17881562]
[[Category: Homo sapiens]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Carman, C V.]]
[[Category: Chen, X.]]
[[Category: Kim, T D.]]
[[Category: Mi, L.]]
[[Category: Song, G.]]
[[Category: Springer, T A.]]
[[Category: NAG]]
[[Category: SO4]]
[[Category: TRS]]
[[Category: ZN]]
[[Category: cell adhesion]]
[[Category: cell-surface dimerization]]
[[Category: igsf domain]]
[[Category: structural plasticity]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:06:28 2008''