4frw

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

Structural highlights

4frw is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

NECT4_HUMAN Ectodermal dysplasia-pili torti-cutaneous syndactyly syndrome. The disease is caused by variants affecting the gene represented in this entry.

Function

NECT4_HUMAN Seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with NECTIN1. Does not act as receptor for alpha-herpesvirus entry into cells. (Microbial infection) Acts as a receptor for measles virus.[1] [2]

Publication Abstract from PubMed

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.

Nectin ectodomain structures reveal a canonical adhesive interface.,Harrison OJ, Vendome J, Brasch J, Jin X, Hong S, Katsamba PS, Ahlsen G, Troyanovsky RB, Troyanovsky SM, Honig B, Shapiro L Nat Struct Mol Biol. 2012 Aug 19. doi: 10.1038/nsmb.2366. PMID:22902367[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
16 reviews cite this structure
Mechanobiology of collective cell behaviours.
Ladoux et al. (2017)
15 more
55 other articles
No citations found

See Also

References

  1. ↑ Muhlebach MD, Mateo M, Sinn PL, Prufer S, Uhlig KM, Leonard VH, Navaratnarajah CK, Frenzke M, Wong XX, Sawatsky B, Ramachandran S, McCray PB Jr, Cichutek K, von Messling V, Lopez M, Cattaneo R. Adherens junction protein nectin-4 is the epithelial receptor for measles virus. Nature. 2011 Nov 2;480(7378):530-3. doi: 10.1038/nature10639. PMID:22048310 doi:http://dx.doi.org/10.1038/nature10639
  2. ↑ Zhang X, Lu G, Qi J, Li Y, He Y, Xu X, Shi J, Zhang CW, Yan J, Gao GF. Structure of measles virus hemagglutinin bound to its epithelial receptor nectin-4. Nat Struct Mol Biol. 2013 Jan;20(1):67-72. doi: 10.1038/nsmb.2432. Epub 2012 Dec , 2. PMID:23202587 doi:http://dx.doi.org/10.1038/nsmb.2432
  3. ↑ Harrison OJ, Vendome J, Brasch J, Jin X, Hong S, Katsamba PS, Ahlsen G, Troyanovsky RB, Troyanovsky SM, Honig B, Shapiro L. Nectin ectodomain structures reveal a canonical adhesive interface. Nat Struct Mol Biol. 2012 Aug 19. doi: 10.1038/nsmb.2366. PMID:22902367 doi:http://dx.doi.org/10.1038/nsmb.2366

Contents


PDB ID 4frw

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