3g7w

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:01, 6 September 2023) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3g7w.png|left|200px]]
 
-
{{STRUCTURE_3g7w| PDB=3g7w | SCENE= }}
+
==Islet Amyloid Polypeptide (IAPP or Amylin) Residues 1 to 22 fused to Maltose Binding Protein==
 +
<StructureSection load='3g7w' size='340' side='right'caption='[[3g7w]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3g7w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G7W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G7W FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRD_900009:alpha-maltotriose'>PRD_900009</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3g7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g7w OCA], [https://pdbe.org/3g7w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g7w RCSB], [https://www.ebi.ac.uk/pdbsum/3g7w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g7w ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/IAPP_HUMAN IAPP_HUMAN] Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g7/3g7w_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=3g7w ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Islet Amyloid Polypeptide (IAPP or amylin) is a peptide hormone produced and stored in the beta-islet cells of the pancreas along with insulin. IAPP readily forms amyloid fibrils in vitro, and the deposition of fibrillar IAPP has been correlated with the pathology of type II diabetes. The mechanism of the conversion that IAPP undergoes from soluble to fibrillar forms has been unclear. By chaperoning IAPP through fusion to maltose binding protein, we find that IAPP can adopt a alpha-helical structure at residues 8-18 and 22-27 and that molecules of IAPP dimerize. Mutational analysis suggests that this dimerization is on the pathway to fibrillation. The structure suggests how IAPP may heterodimerize with insulin, which we confirmed by protein crosslinking. Taken together, these experiments suggest the helical dimerization of IAPP accelerates fibril formation and that insulin impedes fibrillation by blocking the IAPP dimerization interface.
-
===Islet Amyloid Polypeptide (IAPP or Amylin) Residues 1 to 22 fused to Maltose Binding Protein===
+
Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process.,Wiltzius JJ, Sievers SA, Sawaya MR, Eisenberg D Protein Sci. 2009 Apr 29. PMID:19475663<ref>PMID:19475663</ref>
-
{{ABSTRACT_PUBMED_19475663}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 3g7w" style="background-color:#fffaf0;"></div>
-
[[3g7w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G7W OCA].
+
== References ==
-
 
+
<references/>
-
==See Also==
+
__TOC__
-
*[[Maltose-binding protein|Maltose-binding protein]]
+
</StructureSection>
-
 
+
[[Category: Escherichia coli K-12]]
-
==Reference==
+
[[Category: Homo sapiens]]
-
<ref group="xtra">PMID:019475663</ref><references group="xtra"/>
+
[[Category: Large Structures]]
-
[[Category: Escherichia coli k-12]]
+
[[Category: Eisenberg D]]
-
[[Category: Eisenberg, D.]]
+
[[Category: Sawaya MR]]
-
[[Category: Sawaya, M R.]]
+
[[Category: Wiltzius JJW]]
-
[[Category: Wiltzius, J J.W.]]
+
-
[[Category: Amidation]]
+
-
[[Category: Amyloid]]
+
-
[[Category: Cleavage on pair of basic residue]]
+
-
[[Category: Hormone]]
+
-
[[Category: Native fold for amyloidogenic protein]]
+
-
[[Category: Secreted]]
+
-
[[Category: Sugar binding protein]]
+
-
[[Category: Sugar transport]]
+
-
[[Category: Transport]]
+

Current revision

Islet Amyloid Polypeptide (IAPP or Amylin) Residues 1 to 22 fused to Maltose Binding Protein

PDB ID 3g7w

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3g7w"
Personal tools