1bh7: Difference between revisions

Revision as of 19:09, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1bh7.png

Template:STRUCTURE 1bh7

A LOW ENERGY STRUCTURE FOR THE FINAL CYTOPLASMIC LOOP OF BAND 3, NMR, MINIMIZED AVERAGE STRUCTUREA LOW ENERGY STRUCTURE FOR THE FINAL CYTOPLASMIC LOOP OF BAND 3, NMR, MINIMIZED AVERAGE STRUCTURE

Template:ABSTRACT PUBMED 9709005

About this StructureAbout this Structure

1BH7 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3., Askin D, Bloomberg GB, Chambers EJ, Tanner MJ, Biochemistry. 1998 Aug 18;37(33):11670-8. PMID:9709005

Page seeded by OCA on Mon Jun 30 19:09:47 2008

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OCA

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 {{STRUCTURE_1bh7|  PDB=1bh7  |  SCENE=  }}
-'''A LOW ENERGY STRUCTURE FOR THE FINAL CYTOPLASMIC LOOP OF BAND 3, NMR, MINIMIZED AVERAGE STRUCTURE'''
+===A LOW ENERGY STRUCTURE FOR THE FINAL CYTOPLASMIC LOOP OF BAND 3, NMR, MINIMIZED AVERAGE STRUCTURE===
-==Overview==
+<!--
-The membrane domain of the human red cell anion transport protein, band 3, is too large to be studied by solution nuclear magnetic resonance spectroscopy (NMR), and its amphiphilic nature requires the use of detergents for solubilization. An alternative approach is to divide the protein into smaller (trans-membrane or surface loop) domains for NMR study. We report the structure of a 46-residue synthetic peptide that corresponds to the cytoplasmic surface loop connecting the putative 12th and 13th trans-membrane spans (residues 796-841) in the 14 span model of band 3. This peptide was shown by circular dichroism (CD) to be 38% helical in 30% trifluoroacetic acid. Two regions of helix (one close to the N-terminus of the peptide and one close to the C-terminus of the peptide) were identified by NMR. Long-range nuclear Overhauser effect (NOE) cross-peaks showed the two helices to be in near proximity. The helices were separated by a proline-rich loop that exhibited local order but was mobile with respect to the rest of the peptide. We discuss how the NMR structure of this loop fits the current models of band 3 structure and topology and the results of recent mutagenesis experiments. A cyclic version of this peptide was synthesized and studied by CD, but NMR studies were not possible due to the low solubility of this peptide.
+The line below this paragraph, {{ABSTRACT_PUBMED_9709005}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9709005 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9709005}}
 ==About this Structure==
-BH7 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=1BH7 OCA].
+BH7 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=1BH7 OCA].
 ==Reference==
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 [[Category: Cytoplasmic loop]]
 [[Category: Membrane protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:30:27 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:09:47 2008''