1ic1
From Proteopedia
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| - | [[Image:1ic1.jpg|left|200px]] | + | [[Image:1ic1.jpg|left|200px]] |
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| - | '''THE CRYSTAL STRUCTURE FOR THE N-TERMINAL TWO DOMAINS OF ICAM-1''' | + | {{Structure |
| + | |PDB= 1ic1 |SIZE=350|CAPTION= <scene name='initialview01'>1ic1</scene>, resolution 3.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= IC1-P191* ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''THE CRYSTAL STRUCTURE FOR THE N-TERMINAL TWO DOMAINS OF ICAM-1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IC1 is a [ | + | 1IC1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IC1 OCA]. |
==Reference== | ==Reference== | ||
| - | A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1., Casasnovas JM, Stehle T, Liu JH, Wang JH, Springer TA, Proc Natl Acad Sci U S A. 1998 Apr 14;95(8):4134-9. PMID:[http:// | + | A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1., Casasnovas JM, Stehle T, Liu JH, Wang JH, Springer TA, Proc Natl Acad Sci U S A. 1998 Apr 14;95(8):4134-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9539702 9539702] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: immunoglobulin fold]] | [[Category: immunoglobulin fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:48:19 2008'' |
Revision as of 09:48, 20 March 2008
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| , resolution 3.0Å | |||||||
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| Ligands: | |||||||
| Gene: | IC1-P191* (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE FOR THE N-TERMINAL TWO DOMAINS OF ICAM-1
Contents |
Overview
The 3.0-A structure of a 190-residue fragment of intercellular adhesion molecule-1 (ICAM-1, CD54) reveals two tandem Ig-superfamily (IgSF) domains. Each of two independent molecules dimerizes identically with a symmetry-related molecule over a hydrophobic interface on the BED sheet of domain 1, in agreement with dimerization of ICAM-1 on the cell surface. The residues that bind to the integrin LFA-1 are well oriented for bivalent binding in the dimer, with the critical Glu-34 residues pointing away from each other on the periphery. Residues that bind to rhinovirus are in the flexible BC and FG loops at the tip of domain 1, and these and the upper half of domain 1 are well exposed in the dimer for docking to virus. By contrast, a residue important for binding to Plasmodium falciparum-infected erythrocytes is in the dimer interface. The presence of A' strands in both domains 1 and 2, conserved hydrogen bonds at domain junctions, and elaborate hydrogen bond networks around the key integrin binding residues in domain 1 make these domains suited to resist tensile forces during adhesive interactions. A subdivision of the intermediate (I) set of IgSF domains is proposed in which domain 1 of ICAM-1 and previously described I set domains belong to the I1 set and domain 2 of ICAM-1, ICAM-2, and vascular cell adhesion molecule-1 belong to the I2 set.
Disease
Known disease associated with this structure: Malaria, cerebral, susceptibility to OMIM:[147840]
About this Structure
1IC1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1., Casasnovas JM, Stehle T, Liu JH, Wang JH, Springer TA, Proc Natl Acad Sci U S A. 1998 Apr 14;95(8):4134-9. PMID:9539702
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