4FS0
Crystal structure of mutant F136D of mouse nectin-2 extracellular fragment D1-D2
Summary for 4FS0
| Entry DOI | 10.2210/pdb4fs0/pdb |
| Related | 4FMF 4FMK 4FN0 4FOM 4FQP 4FRW |
| Descriptor | Poliovirus receptor-related protein 2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | immunoglobulin-like domain, ig domain, viral entry receptor, cell adhesion |
| Biological source | Mus musculus (mouse) |
| Cellular location | Cell membrane; Single-pass type I membrane protein: P32507 |
| Total number of polymer chains | 1 |
| Total formula weight | 25554.60 |
| Authors | Harrison, O.J.,Brasch, J.,Shapiro, L. (deposition date: 2012-06-26, release date: 2012-08-22, Last modification date: 2024-10-30) |
| Primary citation | Harrison, O.J.,Vendome, J.,Brasch, J.,Jin, X.,Hong, S.,Katsamba, P.S.,Ahlsen, G.,Troyanovsky, R.B.,Troyanovsky, S.M.,Honig, B.,Shapiro, L. Nectin ectodomain structures reveal a canonical adhesive interface. Nat.Struct.Mol.Biol., 19:906-915, 2012 Cited by PubMed Abstract: Nectins are immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues. Homophilic and heterophilic interactions between nectin family members help mediate tissue patterning. We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern. To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5. All of the crystal structures revealed dimeric nectins bound through a stereotyped interface that was previously proposed to represent a cis dimer. However, conservation of this interface and the results of targeted cross-linking experiments showed that this dimer probably represents the adhesive trans interaction. The structure of the dimer provides a simple molecular explanation for the adhesive binding specificity of nectins. PubMed: 22902367DOI: 10.1038/nsmb.2366 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.25 Å) |
Structure validation
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