1w0a: Difference between revisions

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-{{Seed}}
-[[Image:1w0a.png|left|200px]]
-<!--
+==Solution structure of the trans form of the human alpha-hemoglobin stabilizing protein (AHSP)==
-The line below this paragraph, containing "STRUCTURE_1w0a", creates the "Structure Box" on the page.
+<StructureSection load='1w0a' size='340' side='right'caption='[[1w0a]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1w0a]] is a 1 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=1W0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W0A FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1w0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0a OCA], [https://pdbe.org/1w0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w0a RCSB], [https://www.ebi.ac.uk/pdbsum/1w0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w0a ProSAT]</span></td></tr>
-{{STRUCTURE_1w0a|  PDB=1w0a  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AHSP_HUMAN AHSP_HUMAN] Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia.<ref>PMID:12066189</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The structure of alpha-hemoglobin stabilizing protein (AHSP), a molecular chaperone for free alpha-hemoglobin, has been determined using NMR spectroscopy. The protein native state shows conformational heterogeneity attributable to the isomerization of the peptide bond preceding a conserved proline residue. The two equally populated cis and trans forms both adopt an elongated antiparallel three alpha-helix bundle fold but display major differences in the loop between the first two helices and at the C terminus of helix 3. Proline to alanine single point mutation of the residue Pro-30 prevents the cis/trans isomerization. The structure of the P30A mutant is similar to the structure of the trans form of AHSP in the loop 1 region. Both the wild-type AHSP and the P30A mutant bind to alpha-hemoglobin, and the wild-type conformational heterogeneity is quenched upon complex formation, suggesting that just one conformation is the active form. Changes in chemical shift observed upon complex formation identify a binding interface comprising the C terminus of helix 1, the loop 1, and the N terminus of helix 2, with the exposed residues Phe-47 and Tyr-51 being attractive targets for molecular recognition. The characteristics of this interface suggest that AHSP binds at the intradimer alpha1beta1 interface in tetrameric HbA.
-===SOLUTION STRUCTURE OF THE TRANS FORM OF THE HUMAN ALPHA-HEMOGLOBIN STABILIZING PROTEIN (AHSP)===
+NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding.,Santiveri CM, Perez-Canadillas JM, Vadivelu MK, Allen MD, Rutherford TJ, Watkins NA, Bycroft M J Biol Chem. 2004 Aug 13;279(33):34963-70. Epub 2004 Jun 3. PMID:15178680<ref>PMID:15178680</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_15178680}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1w0a" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 15178680 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_15178680}}
+__TOC__
+</StructureSection>
-==About this Structure==
-W0A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W0A OCA].
-==Reference==
-NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding., Santiveri CM, Perez-Canadillas JM, Vadivelu MK, Allen MD, Rutherford TJ, Watkins NA, Bycroft M, J Biol Chem. 2004 Aug 13;279(33):34963-70. Epub 2004 Jun 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15178680 15178680]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Allen, M D.]]
+[[Category: Allen MD]]
-[[Category: Bycroft, M.]]
+[[Category: Bycroft M]]
-[[Category: Perez-Canadillas, J M.]]
+[[Category: Perez-Canadillas JM]]
-[[Category: Rutherford, T J.]]
+[[Category: Rutherford TJ]]
-[[Category: Santiveri, C M.]]
+[[Category: Santiveri CM]]
-[[Category: Vadivelu, M K.]]
+[[Category: Vadivelu MK]]
-[[Category: Watkins, N A.]]
+[[Category: Watkins NA]]
-[[Category: Ahsp nmr structure]]
-[[Category: Alpha-hemoglobin binding]]
-[[Category: Alpha-thalassaemia]]
-[[Category: Chaperone]]
-[[Category: Proline cis/trans isomerization]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:50:50 2008''