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6ulm

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Crystal structure of human cadherin 17 EC1-2

Structural highlights

6ulm is a 2 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 2.15Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAD17_HUMAN Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. LI-cadherin may have a role in the morphological organization of liver and intestine. Involved in intestinal peptide transport.^[1]

Publication Abstract from PubMed

The cadherin superfamily of calcium-dependent cell-adhesion proteins has over 100 members in the human genome. All members of the superfamily feature at least a pair of extracellular cadherin (EC) repeats with calcium-binding sites in the EC linker region. The EC repeats across family members form distinct complexes that mediate cellular adhesion. For instance, classical cadherins (five EC repeats) strand-swap their N-termini and exchange tryptophan residues in EC1, while the clustered protocadherins (six EC repeats) use an extended antiparallel `forearm handshake' involving repeats EC1-EC4. The 7D-cadherins, cadherin-16 (CDH16) and cadherin-17 (CDH17), are the most similar to classical cadherins and have seven EC repeats, two of which are likely to have arisen from gene duplication of EC1-2 from a classical ancestor. However, CDH16 and CDH17 lack the EC1 tryptophan residue used by classical cadherins to mediate adhesion. The structure of human CDH17 EC1-2 presented here reveals features that are not seen in classical cadherins and that are incompatible with the EC1 strand-swap mechanism for adhesion. Analyses of crystal contacts, predicted glycosylation and disease-related mutations are presented along with sequence alignments suggesting that the novel features in the CDH17 EC1-2 structure are well conserved. These results hint at distinct adhesive properties for 7D-cadherins.

Crystal structure of the nonclassical cadherin-17 N-terminus and implications for its adhesive binding mechanism.,Gray ME, Sotomayor M Acta Crystallogr F Struct Biol Commun. 2021 Mar 1;77(Pt 3):85-94. doi:, 10.1107/S2053230X21002247. Epub 2021 Mar 4. PMID:33682793^[2]

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

References

↑ Dantzig AH, Hoskins JA, Tabas LB, Bright S, Shepard RL, Jenkins IL, Duckworth DC, Sportsman JR, Mackensen D, Rosteck PR Jr, et al.. Association of intestinal peptide transport with a protein related to the cadherin superfamily. Science. 1994 Apr 15;264(5157):430-3. doi: 10.1126/science.8153632. PMID:8153632 doi:http://dx.doi.org/10.1126/science.8153632
↑ Gray ME, Sotomayor M. Crystal structure of the nonclassical cadherin-17 N-terminus and implications for its adhesive binding mechanism. Acta Crystallogr F Struct Biol Commun. 2021 Mar 1;77(Pt 3):85-94. PMID:33682793 doi:10.1107/S2053230X21002247