Sandbox Reserved 815: Difference between revisions

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The proportion of each structure is 43% of <scene name='56/568013/Alpha_helix/9'>Alpha Helix</scene>(7 helices, 62 residues) and 2% of <scene name='56/568013/Beta_sheet/1'>Beta Sheet</scene> (2 strands, 4 residues).
The proportion of each structure is 43% of <scene name='56/568013/Alpha_helix/9'>Alpha Helix</scene>(7 helices, 62 residues) and 2% of <scene name='56/568013/Beta_sheet/1'>Beta Sheet</scene> (2 strands, 4 residues).


3 residues can have a contact with metals; S132, H140 and D147.
A lot of empty structures are present between helices.
A lot of empty structures are present between helices.
One of the structure is called 3/10 helix (Each amino acid corresponds to a 120° turn in the helix).
One of the structure is called 3/10 helix (Each amino acid corresponds to a 120° turn in the helix).
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There are 3 types of '''non-polymeric''' entities that can bind this domain:cadmium ion, chloride ion, water.
There are 3 types of '''non-polymeric''' entities that can bind this domain: cadmium ion, chloride ion, water.


This domain 3HAF of the human prion can bind <scene name='56/568013/Ligand/1'>Ligand</scene>(copper (II) ions) with high affinity: '''Cd2+''' [http://en.wikipedia.org/wiki/Cadmium cadnium ions] and '''Cl-''' (chloride ion). Moreover, the entire protein can bind a Cu2+ ions on this NH2 tail and this bond can induce '''conformational change''' with a lot of unknown effect. 3 others residues can have a contact with metals; S132, H140 and D147.
This domain 3HAF of the human prion can bind <scene name='56/568013/Ligand/1'>Ligand</scene> (copper (II) ions) with high affinity: [http://en.wikipedia.org/wiki/Cadmium '''Cd2+'''] and '''Cl-''' . Moreover, the entire protein can bind a Cu2+ ion on this NH2 tail and this bond can induce '''conformational changes''' with a lot of unknown effects. 3 others residues can have a contact with metals; S132, H140 and D147.
In fact, the 3haf domain is only one chain with 2 binding sites for residues CD (H40 and D147)and 1 binding domains for CL S132.
In fact, the 3haf domain is only one chain with 2 binding sites for residues CD (H40 and D147)and 1 binding domains for CL S132.


The entire 3HAF domain can interact with [http://en.wikipedia.org/wiki/GRB2 Growth factor receptor-bound protein 2] (GRB2), [http://en.wikipedia.org/wiki/Exoribonuclease exoribonuclease 3](ERI3) and [http://en.wikipedia.org/wiki/Synapsin_I Synapsin I] (SYN1). There are 3 types of non-polymeric entities that can bind this domain:cadmium ion, chloride ion, water.
The entire 3HAF domain can interact with [http://en.wikipedia.org/wiki/GRB2 Growth factor receptor-bound protein 2] (GRB2), [http://en.wikipedia.org/wiki/Exoribonuclease exoribonuclease 3](ERI3) and [http://en.wikipedia.org/wiki/Synapsin_I Synapsin I] (SYN1).
For this domain, two glycosylated sites exist on helix 2 and 3 at Asn181 and Asn197.
For this domain, two [http://en.wikipedia.org/wiki/Glycosylation glycosylated sites] exist on helix 2 and 3 at Asn181 and Asn197.




Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Pierre-Yves Mocaer