2yvc

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2yvc]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YVC FirstGlance]. <br>
<table><tr><td colspan='2'>[[2yvc]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YVC FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gc7|1gc7]], [[1gc6|1gc6]], [[1j19|1j19]], [[1isn|1isn]], [[2d10|2d10]], [[2d11|2d11]]</td></tr>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gc7|1gc7]], [[1gc6|1gc6]], [[1j19|1j19]], [[1isn|1isn]], [[2d10|2d10]], [[2d11|2d11]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yvc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yvc RCSB], [http://www.ebi.ac.uk/pdbsum/2yvc PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yvc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yvc RCSB], [http://www.ebi.ac.uk/pdbsum/2yvc PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/RADI_MOUSE RADI_MOUSE]] Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane. [[http://www.uniprot.org/uniprot/NEP_MOUSE NEP_MOUSE]] Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9 (By similarity). Involved in the degradation of atrial natriuretic factor (ANF). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers.<ref>PMID:20876573</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Hakoshima, T.]]
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[[Category: Hakoshima, T]]
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[[Category: Kitano, K.]]
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[[Category: Kitano, K]]
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[[Category: Terawaki, S.]]
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[[Category: Terawaki, S]]
[[Category: Cell adhesion]]
[[Category: Cell adhesion]]
[[Category: Protein-peptide complex]]
[[Category: Protein-peptide complex]]

Revision as of 20:16, 25 December 2014

Crystal structure of the Radixin FERM domain complexed with the NEP cytoplasmic tail

2yvc, resolution 3.20Å

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