4FRW

Crystal structure of human nectin-4 extracellular fragment D1-D2

Summary for 4FRW

• Entry DOI: 10.2210/pdb4frw/pdb
• Related: 4FMF 4FMK 4FN0 4FOM 4FQP 4FS0
• Descriptor: Poliovirus receptor-related protein 4 (1 entity in total)
• Functional Keywords: immunoglobulin-like domain, ig domain, viral entry receptor, cell adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Single-pass type I membrane protein (Potential). Processed poliovirus receptor-related protein 4: Secreted: Q96NY8
• Total number of polymer chains: 6
• Total formula weight: 140797.21

Authors

Harrison, O.J.,Jin, X.,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

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: 22902367
DOI: 10.1038/nsmb.2366

Experimental method

X-RAY DIFFRACTION (3.5 Å)