2cuo: Difference between revisions

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==Overview==

The crystal structure of a collagen-model peptide [(Pro-Pro-Gly)(9)](3), has been determined at 1.33 A resolution. Diffraction data were collected, at 100 K using synchrotron radiation, which led to the first structural, study of [(Pro-Pro-Gly)(n)](3) under cryogenic conditions. The crystals, belong to the P2(1) space group with cell parameters of a = 25.95, b =, 26.56, c = 80.14 Angstroms and beta = 90.0 degrees. The overall molecular, conformation was consistent with the left-handed 7/2-helical model with an, axial repeat of 20 A for native collagen. A total of 332 water molecules, were found in an asymmetric unit. Proline residues in adjacent, triple-helices exhibited three types of hydrophobic interactions., Furthermore, three types of hydrogen-bonding networks mediated by water, molecules were observed between adjacent triple-helices. These hydrophobic, interactions and hydrogen-bonding networks occurred at intervals of 20, Angstroms along the c-axis based on the previous sub-cell structures, [(Pro-Pro-Gly)(n)](3) (n = 9, 10), which were also seen in the full-cell, structure of [(Pro-Pro-Gly)(10)](3). Five proline residues at the Y, position in the X-Y-Gly triplet were found in a down-puckering, conformation, this being inconsistent with the recently proposed, propensity-based hypothesis. These proline residues were forced to adopt, opposing puckering because of the prevailing hydrophobic interaction, between triple-helices compared with the Pro:Pro stacking interaction, within a triple-helix.

The crystal structure of a collagen-model peptide [(Pro-Pro-Gly)(9)](3) has been determined at 1.33 A resolution. Diffraction data were collected at 100 K using synchrotron radiation, which led to the first structural study of [(Pro-Pro-Gly)(n)](3) under cryogenic conditions. The crystals belong to the P2(1) space group with cell parameters of a = 25.95, b = 26.56, c = 80.14 Angstroms and beta = 90.0 degrees. The overall molecular conformation was consistent with the left-handed 7/2-helical model with an axial repeat of 20 A for native collagen. A total of 332 water molecules were found in an asymmetric unit. Proline residues in adjacent triple-helices exhibited three types of hydrophobic interactions. Furthermore, three types of hydrogen-bonding networks mediated by water molecules were observed between adjacent triple-helices. These hydrophobic interactions and hydrogen-bonding networks occurred at intervals of 20 Angstroms along the c-axis based on the previous sub-cell structures [(Pro-Pro-Gly)(n)](3) (n = 9, 10), which were also seen in the full-cell structure of [(Pro-Pro-Gly)(10)](3). Five proline residues at the Y position in the X-Y-Gly triplet were found in a down-puckering conformation, this being inconsistent with the recently proposed propensity-based hypothesis. These proline residues were forced to adopt opposing puckering because of the prevailing hydrophobic interaction between triple-helices compared with the Pro:Pro stacking interaction within a triple-helix.

==About this Structure==

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==Reference==

Repetitive interactions observed in the crystal structure of a collagen-model peptide, [(Pro-Pro-Gly)9]3., Hongo C, Noguchi K, Okuyama K, Tanaka Y, Nishino N, J Biochem ~~(Tokyo)~~. 2005 Aug;138(2):135-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16091587 16091587]

Repetitive interactions observed in the crystal structure of a collagen-model peptide, [(Pro-Pro-Gly)9]3., Hongo C, Noguchi K, Okuyama K, Tanaka Y, Nishino N, J Biochem. 2005 Aug;138(2):135-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16091587 16091587]

[[Category: Protein complex]]

[[Category: Hongo, C.]]

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[[Category: triple-helix]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The crystal structure of a collagen-model peptide [(Pro-Pro-Gly)(9)](3), has been determined at 1.33 A resolution. Diffraction data were collected, at 100 K using synchrotron radiation, which led to the first structural, study of [(Pro-Pro-Gly)(n)](3) under cryogenic conditions. The crystals, belong to the P2(1) space group with cell parameters of a = 25.95, b =, 26.56, c = 80.14 Angstroms and beta = 90.0 degrees. The overall molecular, conformation was consistent with the left-handed 7/2-helical model with an, axial repeat of 20 A for native collagen. A total of 332 water molecules, were found in an asymmetric unit. Proline residues in adjacent, triple-helices exhibited three types of hydrophobic interactions., Furthermore, three types of hydrogen-bonding networks mediated by water, molecules were observed between adjacent triple-helices. These hydrophobic, interactions and hydrogen-bonding networks occurred at intervals of 20, Angstroms along the c-axis based on the previous sub-cell structures, [(Pro-Pro-Gly)(n)](3) (n = 9, 10), which were also seen in the full-cell, structure of [(Pro-Pro-Gly)(10)](3). Five proline residues at the Y, position in the X-Y-Gly triplet were found in a down-puckering, conformation, this being inconsistent with the recently proposed, propensity-based hypothesis. These proline residues were forced to adopt, opposing puckering because of the prevailing hydrophobic interaction, between triple-helices compared with the Pro:Pro stacking interaction, within a triple-helix.
+The crystal structure of a collagen-model peptide [(Pro-Pro-Gly)(9)](3) has been determined at 1.33 A resolution. Diffraction data were collected at 100 K using synchrotron radiation, which led to the first structural study of [(Pro-Pro-Gly)(n)](3) under cryogenic conditions. The crystals belong to the P2(1) space group with cell parameters of a = 25.95, b = 26.56, c = 80.14 Angstroms and beta = 90.0 degrees. The overall molecular conformation was consistent with the left-handed 7/2-helical model with an axial repeat of 20 A for native collagen. A total of 332 water molecules were found in an asymmetric unit. Proline residues in adjacent triple-helices exhibited three types of hydrophobic interactions. Furthermore, three types of hydrogen-bonding networks mediated by water molecules were observed between adjacent triple-helices. These hydrophobic interactions and hydrogen-bonding networks occurred at intervals of 20 Angstroms along the c-axis based on the previous sub-cell structures [(Pro-Pro-Gly)(n)](3) (n = 9, 10), which were also seen in the full-cell structure of [(Pro-Pro-Gly)(10)](3). Five proline residues at the Y position in the X-Y-Gly triplet were found in a down-puckering conformation, this being inconsistent with the recently proposed propensity-based hypothesis. These proline residues were forced to adopt opposing puckering because of the prevailing hydrophobic interaction between triple-helices compared with the Pro:Pro stacking interaction within a triple-helix.
 ==About this Structure==
@@ Line 10: / Line 10: @@
 ==Reference==
-Repetitive interactions observed in the crystal structure of a collagen-model peptide, [(Pro-Pro-Gly)9]3., Hongo C, Noguchi K, Okuyama K, Tanaka Y, Nishino N, J Biochem (Tokyo). 2005 Aug;138(2):135-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16091587 16091587]
+Repetitive interactions observed in the crystal structure of a collagen-model peptide, [(Pro-Pro-Gly)9]3., Hongo C, Noguchi K, Okuyama K, Tanaka Y, Nishino N, J Biochem. 2005 Aug;138(2):135-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16091587 16091587]
 [[Category: Protein complex]]
 [[Category: Hongo, C.]]
@@ Line 21: / Line 21: @@
 [[Category: triple-helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:48:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:52:35 2008''