1xfa: Difference between revisions

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[[Image:1xfa.gif|left|200px]]<br /><applet load="1xfa" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1xfa.gif|left|200px]]<br /><applet load="1xfa" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1xfa, resolution 3.10Å" />

'''Structure of NBD1 from murine CFTR- F508R mutant'''<br />

==Overview==

Mutations in the cystic fibrosis transmembrane conductance regulator, (CFTR), an integral membrane protein, cause cystic fibrosis (CF). The most, common CF-causing mutant, deletion of Phe508, fails to properly fold. To, elucidate the role Phe508 plays in the folding of CFTR, missense mutations, at this position were generated. Only one missense mutation had a, pronounced effect on the stability and folding of the isolated domain in, vitro. In contrast, many substitutions, including those of charged and, bulky residues, disrupted folding of full-length CFTR in cells. Structures, of two mutant nucleotide-binding domains (NBDs) reveal only local, alterations of the surface near position 508. These results suggest that, the peptide backbone plays a role in the proper folding of the domain, whereas the side chain plays a role in defining a surface of NBD1 that, potentially interacts with other domains during the maturation of intact, CFTR.

Mutations in the cystic fibrosis transmembrane conductance regulator (CFTR), an integral membrane protein, cause cystic fibrosis (CF). The most common CF-causing mutant, deletion of Phe508, fails to properly fold. To elucidate the role Phe508 plays in the folding of CFTR, missense mutations at this position were generated. Only one missense mutation had a pronounced effect on the stability and folding of the isolated domain in vitro. In contrast, many substitutions, including those of charged and bulky residues, disrupted folding of full-length CFTR in cells. Structures of two mutant nucleotide-binding domains (NBDs) reveal only local alterations of the surface near position 508. These results suggest that the peptide backbone plays a role in the proper folding of the domain, whereas the side chain plays a role in defining a surface of NBD1 that potentially interacts with other domains during the maturation of intact CFTR.

==About this Structure==

1XFA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MG, CL, ATP and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1XFA OCA].

1XFA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFA OCA].

==Reference==

Line 13:

[[Category: Mus musculus]]

[[Category: Single protein]]

[[Category: Brautigam, C.A.]]

[[Category: Brautigam, C A.]]

[[Category: Machius, M.]]

[[Category: Thibodeau, P.H.]]

[[Category: Thibodeau, P H.]]

[[Category: Thomas, P.J.]]

[[Category: Thomas, P J.]]

[[Category: ACY]]

[[Category: ATP]]

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[[Category: nucleotide-binding domain]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 06:02:~~18 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:54:10 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1xfa.gif|left|200px]]<br /><applet load="1xfa" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1xfa.gif|left|200px]]<br /><applet load="1xfa" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1xfa, resolution 3.10&Aring;" />
 '''Structure of NBD1 from murine CFTR- F508R mutant'''<br />
 ==Overview==
-Mutations in the cystic fibrosis transmembrane conductance regulator, (CFTR), an integral membrane protein, cause cystic fibrosis (CF). The most, common CF-causing mutant, deletion of Phe508, fails to properly fold. To, elucidate the role Phe508 plays in the folding of CFTR, missense mutations, at this position were generated. Only one missense mutation had a, pronounced effect on the stability and folding of the isolated domain in, vitro. In contrast, many substitutions, including those of charged and, bulky residues, disrupted folding of full-length CFTR in cells. Structures, of two mutant nucleotide-binding domains (NBDs) reveal only local, alterations of the surface near position 508. These results suggest that, the peptide backbone plays a role in the proper folding of the domain, whereas the side chain plays a role in defining a surface of NBD1 that, potentially interacts with other domains during the maturation of intact, CFTR.
+Mutations in the cystic fibrosis transmembrane conductance regulator (CFTR), an integral membrane protein, cause cystic fibrosis (CF). The most common CF-causing mutant, deletion of Phe508, fails to properly fold. To elucidate the role Phe508 plays in the folding of CFTR, missense mutations at this position were generated. Only one missense mutation had a pronounced effect on the stability and folding of the isolated domain in vitro. In contrast, many substitutions, including those of charged and bulky residues, disrupted folding of full-length CFTR in cells. Structures of two mutant nucleotide-binding domains (NBDs) reveal only local alterations of the surface near position 508. These results suggest that the peptide backbone plays a role in the proper folding of the domain, whereas the side chain plays a role in defining a surface of NBD1 that potentially interacts with other domains during the maturation of intact CFTR.
 ==About this Structure==
-XFA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MG, CL, ATP and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XFA OCA].
+XFA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFA OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Mus musculus]]
 [[Category: Single protein]]
-[[Category: Brautigam, C.A.]]
+[[Category: Brautigam, C A.]]
 [[Category: Machius, M.]]
-[[Category: Thibodeau, P.H.]]
+[[Category: Thibodeau, P H.]]
-[[Category: Thomas, P.J.]]
+[[Category: Thomas, P J.]]
 [[Category: ACY]]
 [[Category: ATP]]
@@ Line 26: / Line 26: @@
 [[Category: nucleotide-binding domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:02:18 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:54:10 2008''