1jy2: Difference between revisions

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Crystal Structure of the Central Region of Bovine Fibrinogen (E5 fragment) at 1.4 Angstroms Resolution

OverviewOverview

The high-resolution crystal structure of the N-terminal central region of bovine fibrinogen (a 35-kDa E(5) fragment) reveals a remarkable dimeric design. The two halves of the molecule bond together at the center in an extensive molecular "handshake" by using both disulfide linkages and noncovalent contacts. On one face of the fragment, the Aalpha and Bbeta chains from the two monomers form a funnel-shaped domain with an unusual hydrophobic cavity; here, on each of the two outer sides there appears to be a binding site for thrombin. On the opposite face, the N-terminal gamma chains fold into a separate domain. Despite the chemical identity of the two halves of fibrinogen, an unusual pair of adjacent disulfide bonds locally constrain the two gamma chains to adopt different conformations. The striking asymmetry of this domain may promote the known supercoiling of the protofibrils in fibrin. This information on the detailed topology of the E(5) fragment permits the construction of a more detailed model than previously possible for the critical trimolecular junction of the protofibril in fibrin.

About this StructureAbout this Structure

1JY2 is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-A resolution., Madrazo J, Brown JH, Litvinovich S, Dominguez R, Yakovlev S, Medved L, Cohen C, Proc Natl Acad Sci U S A. 2001 Oct 9;98(21):11967-72. PMID:11593005

Page seeded by OCA on Thu Feb 21 13:27:59 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1jy2.jpg|left|200px]]<br /><applet load="1jy2" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1jy2.jpg|left|200px]]<br /><applet load="1jy2" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1jy2, resolution 1.4&Aring;" />
 '''Crystal Structure of the Central Region of Bovine Fibrinogen (E5 fragment) at 1.4 Angstroms Resolution'''<br />
 ==Overview==
-The high-resolution crystal structure of the N-terminal central region of, bovine fibrinogen (a 35-kDa E(5) fragment) reveals a remarkable dimeric, design. The two halves of the molecule bond together at the center in an, extensive molecular "handshake" by using both disulfide linkages and, noncovalent contacts. On one face of the fragment, the Aalpha and Bbeta, chains from the two monomers form a funnel-shaped domain with an unusual, hydrophobic cavity; here, on each of the two outer sides there appears to, be a binding site for thrombin. On the opposite face, the N-terminal gamma, chains fold into a separate domain. Despite the chemical identity of the, two halves of fibrinogen, an unusual pair of adjacent disulfide bonds, locally constrain the two gamma chains to adopt different conformations., The striking asymmetry of this domain may promote the known supercoiling, of the protofibrils in fibrin. This information on the detailed topology, of the E(5) fragment permits the construction of a more detailed model, than previously possible for the critical trimolecular junction of the, protofibril in fibrin.
+The high-resolution crystal structure of the N-terminal central region of bovine fibrinogen (a 35-kDa E(5) fragment) reveals a remarkable dimeric design. The two halves of the molecule bond together at the center in an extensive molecular "handshake" by using both disulfide linkages and noncovalent contacts. On one face of the fragment, the Aalpha and Bbeta chains from the two monomers form a funnel-shaped domain with an unusual hydrophobic cavity; here, on each of the two outer sides there appears to be a binding site for thrombin. On the opposite face, the N-terminal gamma chains fold into a separate domain. Despite the chemical identity of the two halves of fibrinogen, an unusual pair of adjacent disulfide bonds locally constrain the two gamma chains to adopt different conformations. The striking asymmetry of this domain may promote the known supercoiling of the protofibrils in fibrin. This information on the detailed topology of the E(5) fragment permits the construction of a more detailed model than previously possible for the critical trimolecular junction of the protofibril in fibrin.
 ==About this Structure==
-JY2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JY2 OCA].
+JY2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JY2 OCA].
 ==Reference==
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 [[Category: Bos taurus]]
 [[Category: Protein complex]]
-[[Category: Brown, J.H.]]
+[[Category: Brown, J H.]]
 [[Category: Cohen, C.]]
 [[Category: Dominguez, R.]]
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 [[Category: fragment e]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:40:52 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:27:59 2008''