1IDN

MAC-1 I DOMAIN METAL FREE

Summary for 1IDN

• Entry DOI: 10.2210/pdb1idn/pdb
• Descriptor: CD11B (2 entities in total)
• Functional Keywords: cell adhesion, integrin, i domain
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 43379.67

Authors

Baldwin, E.T. (deposition date: 1998-06-10, release date: 1998-11-04, Last modification date: 2024-10-16)

Primary citation

Baldwin, E.T.,Sarver, R.W.,Bryant Jr., G.L.,Curry, K.A.,Fairbanks, M.B.,Finzel, B.C.,Garlick, R.L.,Heinrikson, R.L.,Horton, N.C.,Kelley, L.L.,Mildner, A.M.,Moon, J.B.,Mott, J.E.,Mutchler, V.T.,Tomich, C.S.,Watenpaugh, K.D.,Wiley, V.H.
Cation binding to the integrin CD11b I domain and activation model assessment
Structure, 6:923-935, 1998

PubMed Abstract: The integrin family of cell-surface receptors mediate cell adhesion through interactions with the extracellular matrix or other cell-surface receptors. The alpha chain of some integrin heterodimers includes an inserted 'I domain' of about 200 amino acids which binds divalent metal ions and is essential for integrin function. Lee et al. proposed that the I domain of the integrin CD11b adopts a unique 'active' conformation when bound to its counter receptor. In addition, they proposed that the lack of adhesion in the presence of Ca2+ ion reflected the stabilization of an 'inactive' I-domain conformation. We set out to independently determine the structure of the CD11 b I domain and to evaluate the structural effects of divalent ion binding to this protein.

PubMed: 9687375
DOI: 10.1016/S0969-2126(98)00093-8

Experimental method

X-RAY DIFFRACTION (2.7 Å)