1bz0: Difference between revisions
New page: left|200px<br /> <applet load="1bz0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bz0, resolution 1.50Å" /> '''HEMOGLOBIN A (HUMAN... |
No edit summary |
||
| Line 6: | Line 6: | ||
==Overview== | ==Overview== | ||
Hemoglobin Catonsville is a mutation of human hemoglobin (an alpha 2 beta, 2 tetramer) in which a glutamate residue is inserted into the first turn, of a highly conserved 3(10) helix (the C helix) of each alpha subunit. In, theory, amino acid insertions (or deletions) in protein helices can be, accommodated via two distinct mechanisms. One, termed the register shift, mechanism, preserves the geometry of the helix while requiring all of the, residues on one flank of the insertion site to rotate by 100 degrees in, the case of an alpha helix or by 120 degrees in the case of a 3(10) helix., The other, termed the bulge (or indentation) mechanism, distorts the local, geometry of the helix but does not alter the helix register., High-resolution X-ray diffraction analysis of deoxyhemoglobin Catonsville, shows that the inserted residue is accommodated as a bulge, demonstrating, that this is a viable mechanism. (In contrast, no such evidence is yet, available for the register shift mechanism.) More specifically, the, insertion converts one turn of the C helix from 3(10) geometry to alpha, helix-like geometry, raising the possibility that a common mechanism for, accommodating insertions and deletions within helices may involve, localized interconversions between 3(10), alpha, and pi helical, structures. | Hemoglobin Catonsville is a mutation of human hemoglobin (an alpha 2 beta, 2 tetramer) in which a glutamate residue is inserted into the first turn, of a highly conserved 3(10) helix (the C helix) of each alpha subunit. In, theory, amino acid insertions (or deletions) in protein helices can be, accommodated via two distinct mechanisms. One, termed the register shift, mechanism, preserves the geometry of the helix while requiring all of the, residues on one flank of the insertion site to rotate by 100 degrees in, the case of an alpha helix or by 120 degrees in the case of a 3(10) helix., The other, termed the bulge (or indentation) mechanism, distorts the local, geometry of the helix but does not alter the helix register., High-resolution X-ray diffraction analysis of deoxyhemoglobin Catonsville, shows that the inserted residue is accommodated as a bulge, demonstrating, that this is a viable mechanism. (In contrast, no such evidence is yet, available for the register shift mechanism.) More specifically, the, insertion converts one turn of the C helix from 3(10) geometry to alpha, helix-like geometry, raising the possibility that a common mechanism for, accommodating insertions and deletions within helices may involve, localized interconversions between 3(10), alpha, and pi helical, structures. | ||
==Disease== | |||
Known diseases associated with this structure: Erythremias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Erythremias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Erythrocytosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], HPFH, deletion type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Heinz body anemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Heinz body anemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Heinz body anemias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Hemoglobin H disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Hypochromic microcytic anemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Methemoglobinemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Methemoglobinemias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Sickle cell anemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Thalassemia, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Thalassemia-beta, dominant inclusion-body OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Thalassemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Thalassemias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]] | |||
==About this Structure== | ==About this Structure== | ||
| Line 19: | Line 22: | ||
[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:15:43 2007'' | ||
Revision as of 17:09, 12 November 2007
|
HEMOGLOBIN A (HUMAN, DEOXY, HIGH SALT)
OverviewOverview
Hemoglobin Catonsville is a mutation of human hemoglobin (an alpha 2 beta, 2 tetramer) in which a glutamate residue is inserted into the first turn, of a highly conserved 3(10) helix (the C helix) of each alpha subunit. In, theory, amino acid insertions (or deletions) in protein helices can be, accommodated via two distinct mechanisms. One, termed the register shift, mechanism, preserves the geometry of the helix while requiring all of the, residues on one flank of the insertion site to rotate by 100 degrees in, the case of an alpha helix or by 120 degrees in the case of a 3(10) helix., The other, termed the bulge (or indentation) mechanism, distorts the local, geometry of the helix but does not alter the helix register., High-resolution X-ray diffraction analysis of deoxyhemoglobin Catonsville, shows that the inserted residue is accommodated as a bulge, demonstrating, that this is a viable mechanism. (In contrast, no such evidence is yet, available for the register shift mechanism.) More specifically, the, insertion converts one turn of the C helix from 3(10) geometry to alpha, helix-like geometry, raising the possibility that a common mechanism for, accommodating insertions and deletions within helices may involve, localized interconversions between 3(10), alpha, and pi helical, structures.
DiseaseDisease
Known diseases associated with this structure: Erythremias, alpha- OMIM:[141800], Erythremias, beta- OMIM:[141900], Erythrocytosis OMIM:[141850], HPFH, deletion type OMIM:[141900], Heinz body anemia OMIM:[141850], Heinz body anemias, alpha- OMIM:[141800], Heinz body anemias, beta- OMIM:[141900], Hemoglobin H disease OMIM:[141850], Hypochromic microcytic anemia OMIM:[141850], Methemoglobinemias, alpha- OMIM:[141800], Methemoglobinemias, beta- OMIM:[141900], Sickle cell anemia OMIM:[141900], Thalassemia, alpha- OMIM:[141850], Thalassemia-beta, dominant inclusion-body OMIM:[141900], Thalassemias, alpha- OMIM:[141800], Thalassemias, beta- OMIM:[141900]
About this StructureAbout this Structure
1BZ0 is a Protein complex structure of sequences from Homo sapiens with HEM as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Accommodation of insertions in helices: the mutation in hemoglobin Catonsville (Pro 37 alpha-Glu-Thr 38 alpha) generates a 3(10)-->alpha bulge., Kavanaugh JS, Moo-Penn WF, Arnone A, Biochemistry. 1993 Mar 16;32(10):2509-13. PMID:8448109
Page seeded by OCA on Mon Nov 12 16:15:43 2007