Sandbox Reserved 779: Difference between revisions

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My protein is beta-lactoglobulin.
My protein is beta-lactoglobulin.


β-Lac


<big>'''β-Lactoglobulin'''</big>
----
[[Image:structure2D.gif |thumb|left|230px|Human Merlin FERM Domains colored by chain]]
==Introduction ==
1. Introduction
1. Introduction


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Lipocalins have been associated with many biological processes, among them immune response, pheromone transport, biological prostaglandin synthesis, retinoid binding, and cancer cell interactions.
Lipocalins have been associated with many biological processes, among them immune response, pheromone transport, biological prostaglandin synthesis, retinoid binding, and cancer cell interactions.


short description of protein fold: They share limited regions of sequence homology and a common tertiary structure architecture.[2][3][4][5][6] This is an eight stranded antiparallel beta-barrel with a repeated + 1 topology enclosing an internal ligand binding site.[5][4]
short description of protein fold: They share limited regions of sequence homology and a common tertiary structure architecture.[2][3][4][5][6] This is an eight stranded antiparallel beta-barrel with a repeated + 1 topology enclosing an internal ligand binding site.[5][4].<ref>PMID:3125435</ref>
 
Therefore  To know more abouts and the related deseases you can follow the link that leads you to [http://swissvar.expasy.org/cgi-bin/swissvar/result?global_textfield=merlin the Portal to Swiss-Prot diseases and variants ]
organisms:These proteins are found in gram negative bacteria, vertebrate cells, and invertebrate cells, and in plants.  
organisms:These proteins are found in gram negative bacteria, vertebrate cells, and invertebrate cells, and in plants.  


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Allergenic properties:Causes an allergic reaction in human. Is one of the causes of cow's milk allergy.
Allergenic properties:Causes an allergic reaction in human. Is one of the causes of cow's milk allergy.
Miscellaneous The B variant sequence is shown.
Miscellaneous The B variant sequence is shown.
==ERM Proteins==
The merlin-1 protein belongs to the band 4.1 superfamily of membrane-cytoskeletal linkers <ref>PMID:8242753</ref>.
Within this superfamily merlin-1 is closer to ezrin,radixin and moesin (the ERM proteins).
ERM proteins link adehrens junctions to the actin cytoskeleton,and are able to remodel adherens junctions during epithelial morphogenesis.
They also maintain the organization of apical surfaces on the plasma membrane <ref>PMID:11329377</ref>.


2. Structure
2. Structure
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e. methods used to solve the structure : X-ray crystallography, NMR, EM
e. methods used to solve the structure : X-ray crystallography, NMR, EM


[[http://pdb.org/pdb/images/2q2m_asr_r_500.jpg]]


upload the structure (number code: 2Q2M)
upload the structure (number code: 2Q2M)
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at least 5
at least 5


<big>'''Human Merlin FERM Domain'''</big>
----


[[Image:structure2D.gif |thumb|left|230px|Human Merlin FERM Domains colored by chain]]
==Introduction ==
The merlin-1 protein is encoded by the Neurofibromatosis-2(Nf2) gene. Mutations in the Nf2 gene lead to an inheritable autosomal dominant disorder : the Neurofibromatosis type 2. This desease is characterized by tumor proliferations as well in humans as in mice. 
Patients develop tumors of the nervous system : meningiomas, schwannomas, neurofibromas.<ref>PMID:3125435</ref>
Therefore Merlin-1 is a tumor suppressor protein. To know more about the type of Nf2 mutations and the related deseases you can follow the link that leads you to [http://swissvar.expasy.org/cgi-bin/swissvar/result?global_textfield=merlin the Portal to Swiss-Prot diseases and variants ]
==ERM Proteins==
The merlin-1 protein belongs to the band 4.1 superfamily of membrane-cytoskeletal linkers <ref>PMID:8242753</ref>.
Within this superfamily merlin-1 is closer to ezrin,radixin and moesin (the ERM proteins).
ERM proteins link adehrens junctions to the actin cytoskeleton,and are able to remodel adherens junctions during epithelial morphogenesis.
They also maintain the organization of apical surfaces on the plasma membrane <ref>PMID:11329377</ref>.
===Structural organization===
===Structural organization===
All these proteins have an about 300-residue globular plasma membrane-associated  FERM domain(four-point-one ezrin, radixin, moesin).This FERM domain is a highly conserved domain and is divided into three subdomains (F1, F2, and F3).
All these proteins have an about 300-residue globular plasma membrane-associated  FERM domain(four-point-one ezrin, radixin, moesin).This FERM domain is a highly conserved domain and is divided into three subdomains (F1, F2, and F3).