2M32
Alpha-1 integrin I-domain in complex with GLOGEN triple helical peptide
Summary for 2M32
| Entry DOI | 10.2210/pdb2m32/pdb |
| NMR Information | BMRB: 18942 |
| Descriptor | Integrin alpha-1, GLOGEN peptide, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | alpha-1 integrin, i-domain, glogen, cell adhesion |
| Biological source | Homo sapiens (human) More |
| Cellular location | Membrane; Single-pass type I membrane protein: P56199 |
| Total number of polymer chains | 4 |
| Total formula weight | 27423.82 |
| Authors | Chin, Y.,Headey, S.,Mohanty, B.,McEwan, P.,Swarbrick, J.,Mulhern, T.,Emsley, J.,Simpson, J.,Scanlon, M. (deposition date: 2013-01-07, release date: 2013-11-06, Last modification date: 2025-03-26) |
| Primary citation | Chin, Y.K.,Headey, S.J.,Mohanty, B.,Patil, R.,McEwan, P.A.,Swarbrick, J.D.,Mulhern, T.D.,Emsley, J.,Simpson, J.S.,Scanlon, M.J. The Structure of Integrin alpha 1I Domain in Complex with a Collagen-mimetic Peptide. J.Biol.Chem., 288:36796-36809, 2013 Cited by PubMed Abstract: We have determined the structure of the human integrin α1I domain bound to a triple-helical collagen peptide. The structure of the α1I-peptide complex was investigated using data from NMR, small angle x-ray scattering, and size exclusion chromatography that were used to generate and validate a model of the complex using the data-driven docking program, HADDOCK (High Ambiguity Driven Biomolecular Docking). The structure revealed that the α1I domain undergoes a major conformational change upon binding of the collagen peptide. This involves a large movement in the C-terminal helix of the αI domain that has been suggested to be the mechanism by which signals are propagated in the intact integrin receptor. The structure suggests a basis for the different binding selectivity observed for the α1I and α2I domains. Mutational data identify residues that contribute to the conformational change observed. Furthermore, small angle x-ray scattering data suggest that at low collagen peptide concentrations the complex exists in equilibrium between a 1:1 and 2:1 α1I-peptide complex. PubMed: 24187131DOI: 10.1074/jbc.M113.480251 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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