1dsl: Difference between revisions
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<StructureSection load='1dsl' size='340' side='right'caption='[[1dsl]], [[Resolution|resolution]] 1.55Å' scene=''> | <StructureSection load='1dsl' size='340' side='right'caption='[[1dsl]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1dsl]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1dsl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DSL FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dsl OCA], [https://pdbe.org/1dsl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dsl RCSB], [https://www.ebi.ac.uk/pdbsum/1dsl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dsl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/CRGB_BOVIN CRGB_BOVIN]] Crystallins are the dominant structural components of the vertebrate eye lens. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 21:34, 10 March 2021
GAMMA B CRYSTALLIN C-TERMINAL DOMAINGAMMA B CRYSTALLIN C-TERMINAL DOMAIN
Structural highlights
Function[CRGB_BOVIN] Crystallins are the dominant structural components of the vertebrate eye lens. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe use protein engineering and crystallography to simulate aspects of the early evolution of beta gamma-crystallins by observing how a single domain oligomerizes in response to changes in a sequence extension. The crystal structure of the C-terminal domain of gamma beta-crystallin with its four-residue C-terminal extension shows that the domain does not form a symmetric homodimer analogous to the two-domain pairing in beta gamma-crystallins. Instead the C-terminal extension now forms heterologous interactions with other domains leading to the solvent exposure of the natural hydrophobic interface with a consequent loss in protein solubility. However, this domain truncated by just the C-terminal tyrosine forms a symmetric homodimer of domains in the crystal lattice. The X-ray structures of two mutant crystallin domains shed light on the evolution of multi-domain proteins.,Norledge BV, Mayr EM, Glockshuber R, Bateman OA, Slingsby C, Jaenicke R, Driessen HP Nat Struct Biol. 1996 Mar;3(3):267-74. PMID:8605629[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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