Sandbox Reserved 1086

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== Introduction ==
== Introduction ==
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Cadherins are transmembrane proteins that mediate adhesion between cells in the solid tissues of animals. The C-caderin's structure suggests a molecular mechanism for adhesion between cells by classical cadherins such as [[1q5b]],[[1q5c]], and [[1q55]]. It provides a new framework for understanding both cis and trans cadherin interactions.
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Cadherins are transmembrane,calcium binding proteins that mediate adhesion between cells in the solid tissues of animals. These proteins form huge adhesion complexes called Desmosomes of which the architecture is still unclear as well as the molecular mechanism(s) through which the adhesion takes place.
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Green fluorescent protein ('''GFP'''), originally isolated from the jellyfish ''Aequorea victoria'' (PDB entry [[1ema]]), fluorsceses green (509nm) when exposed to blue light (395nm and 475nm). It is one of the most important proteins used in biological research because it can be used to tag otherwise invisible gene products of interest and thus observe their existence, location and movement.
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Their expression is a complex and highly regulated process which plays a pivotal role in many biological landscapes from development to invasiveness of some type of tumors. As the most of transmembrane proteins, cadherins have different structural and functional features addressed to their extracellular and intracellular domains (N terminus and C terminus respectively). The outside portion of the protein consists in five ectodomains ''Ig'' like connected by unstructured regions which give a certain flexibility to the structure. The cell-cell adhesion (also called ''trans'' adhesion) occurs, upon the binding of calcium, between cadherins belonging to opposite cells via interaction of these ectodomains. Interaction between neighbours molecules ("Cis" interactions) happens as well as it tightens the desmosomal plaque and prevents its disassembly.The inner domain has a more globular fold and connects the protein to the cytoskeleton forming an high electron density region called ''inner plaque''. C-cadherin's structure here presented, suggests a molecular mechanism for adhesion between cells by classical cadherins such as [[1q5b]],[[1q5c]], and [[1q55]]. It provides a new framework for understanding both cis and trans cadherin interactions.
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Exploring the Structure
Exploring the Structure

Revision as of 16:31, 20 April 2015

This Sandbox is Reserved from 15/04/2015, through 15/06/2015 for use in the course "Protein structure, function and folding" taught by Taru Meri at the University of Helsinki. This reservation includes Sandbox Reserved 1081 through Sandbox Reserved 1090.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Contents

C-cadherin

C-cadherine (PDB entry 1Q5A)

Drag the structure with the mouse to rotate


Exploring the Structure

GFP is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The chromophore, responsible for the fluorescent properties of the protein, is buried inside the beta barrel as part of the central alpha helix passing through the barrel. The forms via spontaneous cyclization and oxidation of three residues in the central alpha helix: -Thr65 (or Ser65)-Tyr66-Gly67. This cyclization and oxidation creates the chromophore's five-membered ring via a new bond between the threonine and the glycine residues [1].

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Abspregram of the 151 species
Abspregram of the 151 species
.png|thumb|right|350px|Abspregram of the 151 species]]

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Abspregram of the 151 species
Abspregram of the 151 species

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Abspregram of the 151 species
Abspregram of the 151 species

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. [[Image: This is a sample scene created with SAT to by Group, and another to make of the protein.

Structural highlights

1q5a is a 2 chain structure with sequence from Mus musculus. The March 2008 RCSB PDB Molecule of the Month feature on Cadherin by David S. Goodsell is 10.2210/rcsb_pdb/mom_2008_3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Resources:FirstGlance, OCA, RCSB, PDBsum


References

  1. ↑ Ormo M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remington SJ. Crystal structure of the Aequorea victoria green fluorescent protein. Science. 1996 Sep 6;273(5280):1392-5. PMID:8703075
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