1w0a: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
== | |||
==Solution structure of the trans form of the human alpha-hemoglobin stabilizing protein (AHSP)== | |||
<StructureSection load='1w0a' size='340' side='right' caption='[[1w0a]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1w0a' size='340' side='right' caption='[[1w0a]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1w0a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W0A FirstGlance]. <br> | <table><tr><td colspan='2'>[[1w0a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W0A FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w09|1w09]], [[1w0b|1w0b]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w09|1w09]], [[1w0b|1w0b]]</td></tr> | ||
<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=1w0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0a OCA], [http://pdbe.org/1w0a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w0a RCSB], [http://www.ebi.ac.uk/pdbsum/1w0a PDBsum]</span></td></tr> | <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=1w0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0a OCA], [http://pdbe.org/1w0a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w0a RCSB], [http://www.ebi.ac.uk/pdbsum/1w0a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1w0a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
Revision as of 21:41, 24 January 2018
Solution structure of the trans form of the human alpha-hemoglobin stabilizing protein (AHSP)Solution structure of the trans form of the human alpha-hemoglobin stabilizing protein (AHSP)
Structural highlights
Function[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.[1] Publication Abstract from PubMedThe 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||