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1p53
From Proteopedia
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| , resolution 3.06Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | ICAM1 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Crystal Structure of ICAM-1 D3-D5 fragment
Contents |
Overview
We have determined the 3.0 A crystal structure of the three C-terminal domains 3-5 (D3-D5) of ICAM-1. Combined with the previously known N-terminal two-domain structure (D1D2), a model of an entire ICAM-1 extracellular fragment has been constructed. This model should represent a general architecture of other ICAM family members, particularly ICAM-3 and ICAM-5. The observed intimate dimerization interaction at D4 and a stiff D4-D5 stem-like architecture provide a good structural explanation for the existence of preformed ICAM-1 cis dimers on the cell membrane. Together with another dimerization interface at D1, a band-like one-dimensional linear cluster of ICAM-1 on an antigen-presenting cell (APC) surface can be envisioned, which might explain the formation of an immunological synapse between an activated T cell and APC which is critical for T cell receptor signaling.
Disease
Known disease associated with this structure: Malaria, cerebral, susceptibility to OMIM:[147840]
About this Structure
1P53 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for dimerization of ICAM-1 on the cell surface., Yang Y, Jun CD, Liu JH, Zhang R, Joachimiak A, Springer TA, Wang JH, Mol Cell. 2004 Apr 23;14(2):269-76. PMID:15099525
Page seeded by OCA on Sun Mar 30 22:54:57 2008
Categories: Homo sapiens | Single protein | Jochimiak, A. | Jun, C D. | Liu, J H. | Springer, T A. | Wang, J H. | Yang, Y. | Zhang, R. | Beta-sheet | Dimer | Igsf domain
