4NUP
Crystal structure of mouse N-cadherin EC1-2 with AA insertion between residues 2 and 3
Summary for 4NUP
| Entry DOI | 10.2210/pdb4nup/pdb |
| Related | 4NUM 4NUQ |
| Descriptor | N-CADHERIN EC1-2, CALCIUM ION (3 entities in total) |
| Functional Keywords | cell adhesion molecule, cell adhesion |
| Biological source | Mus musculus (mouse) |
| Cellular location | Membrane; Single-pass type I membrane protein (By similarity): Q3UIC2 |
| Total number of polymer chains | 3 |
| Total formula weight | 71679.72 |
| Authors | |
| Primary citation | Vendome, J.,Felsovalyi, K.,Song, H.,Yang, Z.,Jin, X.,Brasch, J.,Harrison, O.J.,Ahlsen, G.,Bahna, F.,Kaczynska, A.,Katsamba, P.S.,Edmond, D.,Hubbell, W.L.,Shapiro, L.,Honig, B. Structural and energetic determinants of adhesive binding specificity in type I cadherins. Proc.Natl.Acad.Sci.USA, 111:E4175-E4184, 2014 Cited by PubMed Abstract: Type I cadherin cell-adhesion proteins are similar in sequence and structure and yet are different enough to mediate highly specific cell-cell recognition phenomena. It has previously been shown that small differences in the homophilic and heterophilic binding affinities of different type I family members can account for the differential cell-sorting behavior. Here we use a combination of X-ray crystallography, analytical ultracentrifugation, surface plasmon resonance and double electron-electron resonance (DEER) electron paramagnetic resonance spectroscopy to identify the molecular determinants of type I cadherin dimerization affinities. Small changes in sequence are found to produce subtle structural and dynamical changes that impact relative affinities, in part via electrostatic and hydrophobic interactions, and in part through entropic effects because of increased conformational heterogeneity in the bound states as revealed by DEER distance mapping in the dimers. These findings highlight the remarkable ability of evolution to exploit a wide range of molecular properties to produce closely related members of the same protein family that have affinity differences finely tuned to mediate their biological roles. PubMed: 25253890DOI: 10.1073/pnas.1416737111 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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