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3FQ4

Crystal structure of the Calx-beta domain of integrin beta4

Summary for 3FQ4
Entry DOI10.2210/pdb3fq4/pdb
Related1QG3 3F7Q 3F7R 3FSO
DescriptorIntegrin beta-4 (2 entities in total)
Functional Keywordsimmunoglobulin fold, integrin, cell adhesion, alternative splicing, disease mutation, epidermolysis bullosa, glycoprotein, membrane, phosphoprotein, polymorphism, receptor, transmembrane
Biological sourceHomo sapiens (Human)
Cellular locationMembrane; Single-pass type I membrane protein: P16144
Total number of polymer chains2
Total formula weight27933.33
Authors
Alonso-Garcia, N.,Ingles-Prieto, A.,de Pereda, J.M. (deposition date: 2009-01-07, release date: 2009-06-23, Last modification date: 2023-11-01)
Primary citationAlonso-Garcia, N.,Ingles-Prieto, A.,Sonnenberg, A.,de Pereda, J.M.
Structure of the Calx-beta domain of the integrin beta4 subunit: insights into function and cation-independent stability
Acta Crystallogr.,Sect.D, 65:858-871, 2009
Cited by
PubMed Abstract: The integrin alpha6beta4 is a receptor for laminins and provides stable adhesion of epithelial cells to the basement membranes. In addition, alpha6beta4 is important for keratinocyte migration during wound healing and favours the invasion of carcinomas into surrounding tissue. The cytoplasmic domain of the beta4 subunit is responsible for most of the intracellular interactions of the integrin; it contains four fibronectin type III domains and a Calx-beta motif. The crystal structure of the Calx-beta domain of beta4 was determined to 1.48 A resolution. The structure does not contain cations and biophysical data support the supposition that the Calx-beta domain of beta4 does not bind calcium. Comparison of the Calx-beta domain of beta4 with the calcium-binding domains of Na(+)/Ca(2+)-exchanger 1 reveals that in beta4 Arg1003 occupies a position equivalent to that of the calcium ions in the Na(+)/Ca(2+)-exchanger. By combining mutagenesis and thermally induced unfolding, it is shown that Arg1003 contributes to the stability of the Calx-beta domain. The structure of the Calx-beta domain is discussed in the context of the function and intracellular interactions of the integrin beta4 subunit and a putative functional site is proposed.
PubMed: 19622870
DOI: 10.1107/S0907444909018745
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.487 Å)
Structure validation

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数据于2024-11-06公开中

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