1n9j

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[[Image:1n9j.png|left|200px]]
 
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==Solution Structure of the 3D domain swapped dimer of Stefin A==
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The line below this paragraph, containing "STRUCTURE_1n9j", creates the "Structure Box" on the page.
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<StructureSection load='1n9j' size='340' side='right'caption='[[1n9j]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1n9j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N9J FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n9j OCA], [https://pdbe.org/1n9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n9j RCSB], [https://www.ebi.ac.uk/pdbsum/1n9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n9j ProSAT]</span></td></tr>
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{{STRUCTURE_1n9j| PDB=1n9j | SCENE= }}
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</table>
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== Disease ==
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'''Solution Structure of the 3D domain swapped dimer of Stefin A'''
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[https://www.uniprot.org/uniprot/CYTA_HUMAN CYTA_HUMAN] Defects in CSTA are the cause of ichthyosis exfoliative autosomal recessive ichthyosis bullosa of Siemens-like (AREI) [MIM:[https://omim.org/entry/607936 607936]. A form of congenital exfoliative ichthyosis, sharing some features with ichthyosis bullosa of Siemens and annular epidermolytic ichthyosis. AREI presents shortly after birth as dry, scaly skin over most of the body with coarse peeling of non-erythematous skin on the palms and soles, which is exacerbated by excessive moisture and minor trauma. Electron microscopy analysis of skin biopsies, reveals mostly normal-appearing upper layers of the epidermis, but prominent intercellular edema of the basal and suprabasal cell layers with aggregates of tonofilaments in the basal keratinocytes.<ref>PMID:21944047</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/CYTA_HUMAN CYTA_HUMAN] This is an intracellular thiol proteinase inhibitor. Has an important role in desmosome-mediated cell-cell adhesion in the lower levels of the epidermis.<ref>PMID:21944047</ref>
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==Overview==
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n9/1n9j_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n9j ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Cystatins, an amyloid-forming structural superfamily, form highly stable, domain-swapped dimers at physiological protein concentrations. In chicken cystatin, the active monomer is a kinetic trap en route to dimerization, and any changes in solution conditions or mutations that destabilize the folded state shorten the lifetime of the monomeric form. In such circumstances, amyloidogenesis will start from conditions where a domain-swapped dimer is the most prevalent species. Domain swapping occurs by a rearrangement of loop I, generating the new intermonomer interface between strands 2 and 3. The transition state for dimerization has a high level of hydrophobic group exposure, indicating that gross conformational perturbation is required for domain swapping to occur. Dimerization also occurs when chicken cystatin is in its reduced, molten-globule state, implying that the organization of secondary structure in this state mirrors that in the folded state and that domain swapping is not limited to the folded states of proteins. Although the interface between cystatin-fold units is poorly defined for cystatin A, the dimers are the appropriate size to account for the electron-dense regions in amyloid protofilaments.
Cystatins, an amyloid-forming structural superfamily, form highly stable, domain-swapped dimers at physiological protein concentrations. In chicken cystatin, the active monomer is a kinetic trap en route to dimerization, and any changes in solution conditions or mutations that destabilize the folded state shorten the lifetime of the monomeric form. In such circumstances, amyloidogenesis will start from conditions where a domain-swapped dimer is the most prevalent species. Domain swapping occurs by a rearrangement of loop I, generating the new intermonomer interface between strands 2 and 3. The transition state for dimerization has a high level of hydrophobic group exposure, indicating that gross conformational perturbation is required for domain swapping to occur. Dimerization also occurs when chicken cystatin is in its reduced, molten-globule state, implying that the organization of secondary structure in this state mirrors that in the folded state and that domain swapping is not limited to the folded states of proteins. Although the interface between cystatin-fold units is poorly defined for cystatin A, the dimers are the appropriate size to account for the electron-dense regions in amyloid protofilaments.
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==About this Structure==
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Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily.,Staniforth RA, Giannini S, Higgins LD, Conroy MJ, Hounslow AM, Jerala R, Craven CJ, Waltho JP EMBO J. 2001 Sep 3;20(17):4774-81. PMID:11532941<ref>PMID:11532941</ref>
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1N9J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N9J OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily., Staniforth RA, Giannini S, Higgins LD, Conroy MJ, Hounslow AM, Jerala R, Craven CJ, Waltho JP, EMBO J. 2001 Sep 3;20(17):4774-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11532941 11532941]
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</div>
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<div class="pdbe-citations 1n9j" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Conroy, M J.]]
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[[Category: Conroy MJ]]
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[[Category: Craven, C J.]]
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[[Category: Craven CJ]]
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[[Category: Giannini, S.]]
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[[Category: Giannini S]]
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[[Category: Higgins, L D.]]
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[[Category: Higgins LD]]
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[[Category: Hounslow, A M.]]
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[[Category: Hounslow AM]]
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[[Category: Jerala, R.]]
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[[Category: Jerala R]]
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[[Category: Staniforth, R A.]]
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[[Category: Staniforth RA]]
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[[Category: Waltho, J P.]]
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[[Category: Waltho JP]]
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[[Category: Amyloid]]
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[[Category: Cystatin]]
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[[Category: Domain swapped]]
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[[Category: Stefin some]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 25 04:51:19 2008''
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Current revision

Solution Structure of the 3D domain swapped dimer of Stefin A

PDB ID 1n9j

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