Sandbox Reserved 779: Difference between revisions
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My protein is beta-lactoglobulin. | My protein is beta-lactoglobulin. | ||
<big>'''β-Lactoglobulin'''</big> | |||
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[[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 | ||
upload the structure (number code: 2Q2M) | upload the structure (number code: 2Q2M) | ||
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at least 5 | at least 5 | ||
===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). | ||